Interaction of DNA with bovine lens α -crystallin: its functional implications
Identifieur interne : 001024 ( Istex/Corpus ); précédent : 001023; suivant : 001025Interaction of DNA with bovine lens α -crystallin: its functional implications
Auteurs : Kamalendra Singh ; B. Groth-Vasselli ; Patricia N. FarnsworthSource :
- International Journal of Biological Macromolecules [ 0141-8130 ] ; 1998.
English descriptors
- Teeft :
- Additional bands, Binding proteins, Biol chem, Biological macromolecules, Consensus motif, Consensus sequence, Crosslinking, Crosslinks subunits, Data show, Dimers trimers, Elsevier science, Faint bands, International journal, Molecular biology, Molecular mass, Normal conditions, Nucl acid, Nuclear function, Orange a6enue, Partial sequences, Phosphate buffer, Physiological stress, Previous studies, Proc natl acad, Protein concentration, Reaction mixtures, Same composition, Secondary structure, Sequence study, Small heat shock proteins, Subunit, Subunits share, Tetramers.
Abstract
Abstract: Under normal conditions, lens aggregates of α-crystallin subunits, αA and αB, are found in the cytoplasm. However, during stress in nonlenticular tissues, αB translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with α-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of α-crystallin subunits. The formation of tetramers appears to modify α-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that α-crystallin may have a nuclear function which includes DNA binding.
Url:
DOI: 10.1016/S0141-8130(98)00029-4
Links to Exploration step
ISTEX:3489EC44A7202C7CB1CF46935C7F73D31415E0C5Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Interaction of DNA with bovine lens α -crystallin: its functional implications</title><author><name sortKey="Singh, Kamalendra" sort="Singh, Kamalendra" uniqKey="Singh K" first="Kamalendra" last="Singh">Kamalendra Singh</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation></author><author><name sortKey="Groth Vasselli, B" sort="Groth Vasselli, B" uniqKey="Groth Vasselli B" first="B." last="Groth-Vasselli">B. Groth-Vasselli</name><affiliation><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation></author><author><name sortKey="Farnsworth, Patricia N" sort="Farnsworth, Patricia N" uniqKey="Farnsworth P" first="Patricia N." last="Farnsworth">Patricia N. Farnsworth</name><affiliation><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:3489EC44A7202C7CB1CF46935C7F73D31415E0C5</idno><date when="1997" year="1997">1997</date><idno type="doi">10.1016/S0141-8130(98)00029-4</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-679VVN73-K/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001024</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001024</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Interaction of DNA with bovine lens α -crystallin: its functional implications</title><author><name sortKey="Singh, Kamalendra" sort="Singh, Kamalendra" uniqKey="Singh K" first="Kamalendra" last="Singh">Kamalendra Singh</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation></author><author><name sortKey="Groth Vasselli, B" sort="Groth Vasselli, B" uniqKey="Groth Vasselli B" first="B." last="Groth-Vasselli">B. Groth-Vasselli</name><affiliation><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation></author><author><name sortKey="Farnsworth, Patricia N" sort="Farnsworth, Patricia N" uniqKey="Farnsworth P" first="Patricia N." last="Farnsworth">Patricia N. Farnsworth</name><affiliation><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">International Journal of Biological Macromolecules</title><title level="j" type="abbrev">BIOMAC</title><idno type="ISSN">0141-8130</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">22</biblScope><biblScope unit="issue">3–4</biblScope><biblScope unit="page" from="315">315</biblScope><biblScope unit="page" to="320">320</biblScope></imprint><idno type="ISSN">0141-8130</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0141-8130</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Additional bands</term><term>Binding proteins</term><term>Biol chem</term><term>Biological macromolecules</term><term>Consensus motif</term><term>Consensus sequence</term><term>Crosslinking</term><term>Crosslinks subunits</term><term>Data show</term><term>Dimers trimers</term><term>Elsevier science</term><term>Faint bands</term><term>International journal</term><term>Molecular biology</term><term>Molecular mass</term><term>Normal conditions</term><term>Nucl acid</term><term>Nuclear function</term><term>Orange a6enue</term><term>Partial sequences</term><term>Phosphate buffer</term><term>Physiological stress</term><term>Previous studies</term><term>Proc natl acad</term><term>Protein concentration</term><term>Reaction mixtures</term><term>Same composition</term><term>Secondary structure</term><term>Sequence study</term><term>Small heat shock proteins</term><term>Subunit</term><term>Subunits share</term><term>Tetramers</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Under normal conditions, lens aggregates of α-crystallin subunits, αA and αB, are found in the cytoplasm. However, during stress in nonlenticular tissues, αB translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with α-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of α-crystallin subunits. The formation of tetramers appears to modify α-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that α-crystallin may have a nuclear function which includes DNA binding.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>crosslinking</json:string><json:string>subunit</json:string><json:string>tetramers</json:string><json:string>consensus sequence</json:string><json:string>biological macromolecules</json:string><json:string>international journal</json:string><json:string>secondary structure</json:string><json:string>phosphate buffer</json:string><json:string>binding proteins</json:string><json:string>subunits share</json:string><json:string>proc natl acad</json:string><json:string>orange a6enue</json:string><json:string>molecular biology</json:string><json:string>dimers trimers</json:string><json:string>additional bands</json:string><json:string>partial sequences</json:string><json:string>protein concentration</json:string><json:string>data show</json:string><json:string>normal conditions</json:string><json:string>nuclear function</json:string><json:string>elsevier science</json:string><json:string>previous studies</json:string><json:string>faint bands</json:string><json:string>same composition</json:string><json:string>molecular mass</json:string><json:string>reaction mixtures</json:string><json:string>small heat shock proteins</json:string><json:string>crosslinks subunits</json:string><json:string>consensus motif</json:string><json:string>physiological stress</json:string><json:string>sequence study</json:string><json:string>nucl acid</json:string><json:string>biol chem</json:string></teeft></keywords><author><json:item><name>Kamalendra Singh</name><affiliations><json:string>Department of Biochemistry and Molecular Biology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</json:string></affiliations></json:item><json:item><name>B. Groth-Vasselli</name><affiliations><json:string>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</json:string></affiliations></json:item><json:item><name>Patricia N. Farnsworth</name><affiliations><json:string>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</json:string><json:string>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</json:string><json:string>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>α-Crystallin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lens</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Single stranded DNA</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Double stranded DNA</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>UV photo-crosslinking</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Small heat shock proteins</value></json:item></subject><arkIstex>ark:/67375/6H6-679VVN73-K</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Under normal conditions, lens aggregates of α-crystallin subunits, αA and αB, are found in the cytoplasm. However, during stress in nonlenticular tissues, αB translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with α-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of α-crystallin subunits. The formation of tetramers appears to modify α-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that α-crystallin may have a nuclear function which includes DNA binding.</abstract><qualityIndicators><score>6.22</score><pdfWordCount>2948</pdfWordCount><pdfCharCount>18095</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>106</abstractWordCount><abstractCharCount>771</abstractCharCount><keywordCount>6</keywordCount></qualityIndicators><title>Interaction of DNA with bovine lens α -crystallin: its functional implications</title><pmid><json:string>9650086</json:string></pmid><pii><json:string>S0141-8130(98)00029-4</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>International Journal of Biological Macromolecules</title><language><json:string>unknown</json:string></language><publicationDate>1998</publicationDate><issn><json:string>0141-8130</json:string></issn><pii><json:string>S0141-8130(00)X0023-2</json:string></pii><volume>22</volume><issue>3–4</issue><pages><first>315</first><last>320</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1997</json:string></date><geogName></geogName><orgName><json:string>Spectronic Corp.</json:string><json:string>Department of Ophthalmology, UMD</json:string><json:string>Department of Biochemistry and Molecular Biology</json:string><json:string>Lions Eye Research Foundation of New Jersey</json:string><json:string>Department of Pharmacology and Physiology</json:string><json:string>Foundation of UMDNJ</json:string></orgName><orgName_funder><json:string>Foundation of UMDNJ</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>N.J. Green</json:string><json:string>Mukund</json:string><json:string>H. Dylan</json:string><json:string>The</json:string><json:string>Provencher</json:string><json:string>J. Modak</json:string><json:string>Glockner</json:string><json:string>Aviv Associates</json:string><json:string>K. Site</json:string></persName><placeName><json:string>Orange</json:string><json:string>Newark</json:string><json:string>NJ</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[4]</json:string><json:string>[12]</json:string><json:string>[18]</json:string><json:string>K. Singh et al.</json:string><json:string>[6]</json:string><json:string>[22]</json:string><json:string>[20,21]</json:string><json:string>[8]</json:string><json:string>[17]</json:string><json:string>[14,15]</json:string><json:string>Pietrowski et al. [5]</json:string><json:string>[10]</json:string><json:string>[16]</json:string><json:string>[3]</json:string><json:string>[5]</json:string><json:string>[7]</json:string><json:string>Ausubel et al. [9]</json:string><json:string>[2]</json:string><json:string>[13]</json:string><json:string>[19]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-679VVN73-K</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - natural sciences</json:string><json:string>2 - chemistry</json:string><json:string>3 - polymers</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Structural Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1998</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1016/S0141-8130(98)00029-4</json:string></doi><id>3489EC44A7202C7CB1CF46935C7F73D31415E0C5</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-679VVN73-K/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-679VVN73-K/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-679VVN73-K/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Interaction of DNA with bovine lens α -crystallin: its functional implications</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1997 Elsevier Science B.V.</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1997</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Fig. 1: (a) Commassie blue staining of SDS-PAGE showing the effect of the UV-exposure on α-crystallin. UV-unexposed (lanes 1 and 2) and UV-exposed (lanes 3 and 4) contain 25 and 50 μM α-crystallin, respectively. In lanes 1–4, two dark bands just above 16 kDa represent αA (lower) and αB (upper) subunits. The bands near 84 kDa in lanes 3 and 4 represent the tetramer of subunits. The faint bands between monomer and tetramer position in lanes 3 and 4 are the dimers and trimers of the subunits. (b) Far UV–CD spectra of UV-exposed (♦) and UV-unexposed (▾) α-crystallin samples.</note><note type="content">Fig. 2: (a) Autoradiogram of SDS-PAGE showing the crosslinking of 37-mer with α-crystallin. Lanes 1–4 contain UV-exposed 10, 25, 50 and 80 μM α-crystallin with 12, 30, 60 and 80 mM KC1, respectively. The sample in lane 5 containing the same composition as lane 1 was not UV-exposed. The bands in lanes 1–4 above 84 kDa represent the crosslinking of the 37-mer with the tetramers of subunits and the faint bands at monomer position probably represent the crosslinking of extraneous ATP with α-crystallin subunit. (b) Coomassie blue staining of SDS-PAGE showing crosslinking of 37-mer. The migration of the bands for monomers (above 16 kDa) in lanes 1–5 is identical. This indicates that the 37-mer does not crosslink with single subunits.</note><note type="content">Fig. 3: (a) Autoradiogram of SDS-PAGE showing the crosslinking of dA36 with α-crystallin. Except for some additional bands between monomer and tetramer positions the crosslinking pattern of dA36 is similar to the 37-mer. The additional bands represent the crosslinking of dA36 with dimers and/or trimers of α-crystallin subunits. (b) Coomassie blue staining of SDS-PAGE corresponding to Fig. 3a.</note><note type="content">Fig. 4: Aligned partial sequences of α-crystallin subunits (αA and αB), Antenopedia homeodomain protein (Antp), Human Engrailed homeodomain protein (Hu-En1), Klenow fragment of polymerase I from E. coli (KF), Human immunodiffeciency virus type 1 reverse transcriptase (HIV1-RT) and rat DNA polymerase β (pol β). The sequences of αA, αB, Antp, Hu-En1 and KF progress from N- to C-terminal while the sequences of HIV1-RT and pol β from C- to N-terminal. It is appropriate to compare those sequences in the reverse order since, during evolution, portions of a protein sequence may be transposed by transposases. This process may maintain and/or modify its original function.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Interaction of DNA with bovine lens α -crystallin: its functional implications</title><author xml:id="author-0000"><persName><forename type="first">Kamalendra</forename><surname>Singh</surname></persName><affiliation>Department of Biochemistry and Molecular Biology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">B.</forename><surname>Groth-Vasselli</surname></persName><affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Patricia N.</forename><surname>Farnsworth</surname></persName><affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation><affiliation>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation><affiliation>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</affiliation></author><idno type="istex">3489EC44A7202C7CB1CF46935C7F73D31415E0C5</idno><idno type="ark">ark:/67375/6H6-679VVN73-K</idno><idno type="DOI">10.1016/S0141-8130(98)00029-4</idno><idno type="PII">S0141-8130(98)00029-4</idno></analytic><monogr><title level="j">International Journal of Biological Macromolecules</title><title level="j" type="abbrev">BIOMAC</title><idno type="pISSN">0141-8130</idno><idno type="PII">S0141-8130(00)X0023-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">22</biblScope><biblScope unit="issue">3–4</biblScope><biblScope unit="page" from="315">315</biblScope><biblScope unit="page" to="320">320</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Under normal conditions, lens aggregates of α-crystallin subunits, αA and αB, are found in the cytoplasm. However, during stress in nonlenticular tissues, αB translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with α-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of α-crystallin subunits. The formation of tetramers appears to modify α-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that α-crystallin may have a nuclear function which includes DNA binding.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>α-Crystallin</term></item><item><term>Lens</term></item><item><term>Single stranded DNA</term></item><item><term>Double stranded DNA</term></item><item><term>UV photo-crosslinking</term></item><item><term>Small heat shock proteins</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-679VVN73-K/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="gr1a" NDATA="IMAGE" name="gr1a"></istex:entity><istex:entity SYSTEM="gr1b" NDATA="IMAGE" name="gr1b"></istex:entity><istex:entity SYSTEM="gr2a" NDATA="IMAGE" name="gr2a"></istex:entity><istex:entity SYSTEM="gr2b" NDATA="IMAGE" name="gr2b"></istex:entity><istex:entity SYSTEM="gr3a" NDATA="IMAGE" name="gr3a"></istex:entity><istex:entity SYSTEM="gr3b" NDATA="IMAGE" name="gr3b"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>BIOMAC</jid><aid>1266</aid><ce:pii>S0141-8130(98)00029-4</ce:pii><ce:doi>10.1016/S0141-8130(98)00029-4</ce:doi><ce:copyright year="1997" type="full-transfer">Elsevier Science B.V.</ce:copyright></item-info><head><ce:title>Interaction of DNA with bovine lens <ce:italic>α</ce:italic>-crystallin: its functional implications</ce:title><ce:author-group><ce:author><ce:given-name>Kamalendra</ce:given-name><ce:surname>Singh</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref></ce:author><ce:author><ce:given-name>B.</ce:given-name><ce:surname>Groth-Vasselli</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref></ce:author><ce:author><ce:given-name>Patricia N.</ce:given-name><ce:surname>Farnsworth</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref><ce:cross-ref refid="AFF3">c</ce:cross-ref><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Biochemistry and Molecular Biology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</ce:text></ce:correspondence></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Under normal conditions, lens aggregates of <ce:italic>α</ce:italic>-crystallin subunits, <ce:italic>α</ce:italic>A and <ce:italic>α</ce:italic>B, are found in the cytoplasm. However, during stress in nonlenticular tissues, <ce:italic>α</ce:italic>B translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with <ce:italic>α</ce:italic>-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of <ce:italic>α</ce:italic>-crystallin subunits. The formation of tetramers appears to modify <ce:italic>α</ce:italic>-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that <ce:italic>α</ce:italic>-crystallin may have a nuclear function which includes DNA binding.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text><ce:italic>α</ce:italic>-Crystallin</ce:text></ce:keyword><ce:keyword><ce:text>Lens</ce:text></ce:keyword><ce:keyword><ce:text>Single stranded DNA</ce:text></ce:keyword><ce:keyword><ce:text>Double stranded DNA</ce:text></ce:keyword><ce:keyword><ce:text>UV photo-crosslinking</ce:text></ce:keyword><ce:keyword><ce:text>Small heat shock proteins</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Interaction of DNA with bovine lens α -crystallin: its functional implications</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Interaction of DNA with bovine lens</title></titleInfo><name type="personal"><namePart type="given">Kamalendra</namePart><namePart type="family">Singh</namePart><affiliation>Department of Biochemistry and Molecular Biology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="family">Groth-Vasselli</namePart><affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Patricia N.</namePart><namePart type="family">Farnsworth</namePart><affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation><affiliation>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</affiliation><affiliation>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Under normal conditions, lens aggregates of α-crystallin subunits, αA and αB, are found in the cytoplasm. However, during stress in nonlenticular tissues, αB translocates to the nucleus. A sequence study revealed that both subunits share a consensus sequence with other DNA binding proteins. These observations prompted us to investigate DNA binding with α-crystallin by UV-mediated photo-crosslinking. The data show that both single and double stranded DNA crosslink mainly with tetramers of α-crystallin subunits. The formation of tetramers appears to modify α-crystallin interactive properties and, therefore, its induction may have functional significance. These observations suggest that α-crystallin may have a nuclear function which includes DNA binding.</abstract><note type="content">Fig. 1: (a) Commassie blue staining of SDS-PAGE showing the effect of the UV-exposure on α-crystallin. UV-unexposed (lanes 1 and 2) and UV-exposed (lanes 3 and 4) contain 25 and 50 μM α-crystallin, respectively. In lanes 1–4, two dark bands just above 16 kDa represent αA (lower) and αB (upper) subunits. The bands near 84 kDa in lanes 3 and 4 represent the tetramer of subunits. The faint bands between monomer and tetramer position in lanes 3 and 4 are the dimers and trimers of the subunits. (b) Far UV–CD spectra of UV-exposed (♦) and UV-unexposed (▾) α-crystallin samples.</note><note type="content">Fig. 2: (a) Autoradiogram of SDS-PAGE showing the crosslinking of 37-mer with α-crystallin. Lanes 1–4 contain UV-exposed 10, 25, 50 and 80 μM α-crystallin with 12, 30, 60 and 80 mM KC1, respectively. The sample in lane 5 containing the same composition as lane 1 was not UV-exposed. The bands in lanes 1–4 above 84 kDa represent the crosslinking of the 37-mer with the tetramers of subunits and the faint bands at monomer position probably represent the crosslinking of extraneous ATP with α-crystallin subunit. (b) Coomassie blue staining of SDS-PAGE showing crosslinking of 37-mer. The migration of the bands for monomers (above 16 kDa) in lanes 1–5 is identical. This indicates that the 37-mer does not crosslink with single subunits.</note><note type="content">Fig. 3: (a) Autoradiogram of SDS-PAGE showing the crosslinking of dA36 with α-crystallin. Except for some additional bands between monomer and tetramer positions the crosslinking pattern of dA36 is similar to the 37-mer. The additional bands represent the crosslinking of dA36 with dimers and/or trimers of α-crystallin subunits. (b) Coomassie blue staining of SDS-PAGE corresponding to Fig. 3a.</note><note type="content">Fig. 4: Aligned partial sequences of α-crystallin subunits (αA and αB), Antenopedia homeodomain protein (Antp), Human Engrailed homeodomain protein (Hu-En1), Klenow fragment of polymerase I from E. coli (KF), Human immunodiffeciency virus type 1 reverse transcriptase (HIV1-RT) and rat DNA polymerase β (pol β). The sequences of αA, αB, Antp, Hu-En1 and KF progress from N- to C-terminal while the sequences of HIV1-RT and pol β from C- to N-terminal. It is appropriate to compare those sequences in the reverse order since, during evolution, portions of a protein sequence may be transposed by transposases. This process may maintain and/or modify its original function.</note><subject><genre>Keywords</genre><topic>α-Crystallin</topic><topic>Lens</topic><topic>Single stranded DNA</topic><topic>Double stranded DNA</topic><topic>UV photo-crosslinking</topic><topic>Small heat shock proteins</topic></subject><relatedItem type="host"><titleInfo><title>International Journal of Biological Macromolecules</title></titleInfo><titleInfo type="abbreviated"><title>BIOMAC</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued></originInfo><identifier type="ISSN">0141-8130</identifier><identifier type="PII">S0141-8130(00)X0023-2</identifier><part><date>1998</date><detail type="volume"><number>22</number><caption>vol.</caption></detail><detail type="issue"><number>3–4</number><caption>no.</caption></detail><extent unit="issue-pages"><start>149</start><end>344</end></extent><extent unit="pages"><start>315</start><end>320</end></extent></part></relatedItem><identifier type="istex">3489EC44A7202C7CB1CF46935C7F73D31415E0C5</identifier><identifier type="ark">ark:/67375/6H6-679VVN73-K</identifier><identifier type="DOI">10.1016/S0141-8130(98)00029-4</identifier><identifier type="PII">S0141-8130(98)00029-4</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Elsevier Science B.V.</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Elsevier Science B.V., ©1997</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-679VVN73-K/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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