Interaction of DNA with bovine lens α -crystallin: its functional implications
Identifieur interne : 001024 ( Istex/Curation ); précédent : 001023; suivant : 001025Interaction of DNA with bovine lens α -crystallin: its functional implications
Auteurs : Kamalendra Singh [États-Unis] ; B. Groth-Vasselli [États-Unis] ; Patricia N. Farnsworth [États-Unis]Source :
- 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
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Groth-Vasselli</name><affiliation wicri:level="1"><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103</wicri:regionArea></affiliation></author><author><name sortKey="Farnsworth, Patricia N" sort="Farnsworth, Patricia N" uniqKey="Farnsworth P" first="Patricia N." last="Farnsworth">Patricia N. 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Groth-Vasselli</name><affiliation wicri:level="1"><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103</wicri:regionArea></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 wicri:level="1"><mods:affiliation>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Ophthalmology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology and Physiology, UMD—New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Corresponding author. Tel.: +1 973 9724489; fax: +1 973 9727950; e-mail: farnswor@umdnj.edu</mods:affiliation><country wicri:rule="url">États-Unis</country></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></record>Pour manipuler ce document sous Unix (Dilib)
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