Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Gao, Feng" sort="Gao, Feng" uniqKey="Gao F" first="Feng" last="Gao">Feng Gao</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kight, Alicia D" sort="Kight, Alicia D" uniqKey="Kight A" first="Alicia D." last="Kight">Alicia D. Kight</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Henderson, Rory" sort="Henderson, Rory" uniqKey="Henderson R" first="Rory" last="Henderson">Rory Henderson</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Jayanthi, Srinivas" sort="Jayanthi, Srinivas" uniqKey="Jayanthi S" first="Srinivas" last="Jayanthi">Srinivas Jayanthi</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Patel, Parth" sort="Patel, Parth" uniqKey="Patel P" first="Parth" last="Patel">Parth Patel</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Murchison, Marissa" sort="Murchison, Marissa" uniqKey="Murchison M" first="Marissa" last="Murchison">Marissa Murchison</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Sharma, Priyanka" sort="Sharma, Priyanka" uniqKey="Sharma P" first="Priyanka" last="Sharma">Priyanka Sharma</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Goforth, Robyn L" sort="Goforth, Robyn L" uniqKey="Goforth R" first="Robyn L." last="Goforth">Robyn L. Goforth</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kumar, Thallapuranam Krishnaswamy Suresh" sort="Kumar, Thallapuranam Krishnaswamy Suresh" uniqKey="Kumar T" first="Thallapuranam Krishnaswamy Suresh" last="Kumar">Thallapuranam Krishnaswamy Suresh Kumar</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Henry, Ralph L" sort="Henry, Ralph L" uniqKey="Henry R" first="Ralph L." last="Henry">Ralph L. Henry</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Heyes, Colin D" sort="Heyes, Colin D" uniqKey="Heyes C" first="Colin D." last="Heyes">Colin D. Heyes</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">25918165</idno>
<idno type="pmc">4505461</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4505461</idno>
<idno type="RBID">PMC:4505461</idno>
<idno type="doi">10.1074/jbc.M114.624346</idno>
<date when="2015">2015</date>
<idno type="wicri:Area/Pmc/Corpus">000042</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Gao, Feng" sort="Gao, Feng" uniqKey="Gao F" first="Feng" last="Gao">Feng Gao</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kight, Alicia D" sort="Kight, Alicia D" uniqKey="Kight A" first="Alicia D." last="Kight">Alicia D. Kight</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Henderson, Rory" sort="Henderson, Rory" uniqKey="Henderson R" first="Rory" last="Henderson">Rory Henderson</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Jayanthi, Srinivas" sort="Jayanthi, Srinivas" uniqKey="Jayanthi S" first="Srinivas" last="Jayanthi">Srinivas Jayanthi</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Patel, Parth" sort="Patel, Parth" uniqKey="Patel P" first="Parth" last="Patel">Parth Patel</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Murchison, Marissa" sort="Murchison, Marissa" uniqKey="Murchison M" first="Marissa" last="Murchison">Marissa Murchison</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Sharma, Priyanka" sort="Sharma, Priyanka" uniqKey="Sharma P" first="Priyanka" last="Sharma">Priyanka Sharma</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Goforth, Robyn L" sort="Goforth, Robyn L" uniqKey="Goforth R" first="Robyn L." last="Goforth">Robyn L. Goforth</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kumar, Thallapuranam Krishnaswamy Suresh" sort="Kumar, Thallapuranam Krishnaswamy Suresh" uniqKey="Kumar T" first="Thallapuranam Krishnaswamy Suresh" last="Kumar">Thallapuranam Krishnaswamy Suresh Kumar</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Henry, Ralph L" sort="Henry, Ralph L" uniqKey="Henry R" first="Ralph L." last="Henry">Ralph L. Henry</name>
<affiliation><nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Heyes, Colin D" sort="Heyes, Colin D" uniqKey="Heyes C" first="Colin D." last="Heyes">Colin D. Heyes</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2015">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
Targeting of proteins requires a signal recognition particle (SRP) and multiple protein interactions.</p>
<p><bold>Results:</bold>
We observed a decrease in the structural dynamics of cpSRP43 and an increase in substrate affinity upon its binding to cpSRP54.</p>
<p><bold>Conclusion:</bold>
Changes in domain dynamics induced by cpSRP subunit interactions mediate substrate affinity.</p>
<p><bold>Significance:</bold>
Relating structure and dynamics of SRP proteins allows for a better understanding of vectorial targeting within cells.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">25918165</article-id>
<article-id pub-id-type="pmc">4505461</article-id>
<article-id pub-id-type="publisher-id">M114.624346</article-id>
<article-id pub-id-type="doi">10.1074/jbc.M114.624346</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Molecular Biophysics</subject>
</subj-group>
</article-categories>
<title-group><article-title>Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</article-title>
<alt-title alt-title-type="short">Interdomain Dynamics of cpSRP43</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Gao</surname>
<given-names>Feng</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kight</surname>
<given-names>Alicia D.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Henderson</surname>
<given-names>Rory</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Jayanthi</surname>
<given-names>Srinivas</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Patel</surname>
<given-names>Parth</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Murchison</surname>
<given-names>Marissa</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Sharma</surname>
<given-names>Priyanka</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Goforth</surname>
<given-names>Robyn L.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kumar</surname>
<given-names>Thallapuranam Krishnaswamy Suresh</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="corresp" rid="cor1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Henry</surname>
<given-names>Ralph L.</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="corresp" rid="cor2"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Heyes</surname>
<given-names>Colin D.</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="corresp" rid="cor3"><sup>3</sup>
</xref>
</contrib>
<aff id="aff1">From the Departments of<label>‡</label>
Chemistry and Biochemistry and</aff>
<aff id="aff2"><label>§</label>
Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>1</label>
To whom correspondence may be addressed: <addr-line>Dept. of Chemistry and Biochemistry, 345 N. Campus Dr., Fayetteville, AR 72701.</addr-line>
Tel.: <phone>479-575-5646</phone>
; Fax: <fax>479-575-4049</fax>
; E-mail: <email>sthalla@uark.edu</email>
.</corresp>
<corresp id="cor2"><label>2</label>
To whom correspondence may be addressed: <addr-line>Dept. of Biological Sciences, 731 W. Dickson St., Fayetteville, AR 72701.</addr-line>
Tel.: <phone>479-575-2529</phone>
; Fax: <fax>479-575-4010</fax>
; E-mail: <email>rahenry@uark.edu</email>
.</corresp>
<corresp id="cor3"><label>3</label>
To whom correspondence may be addressed: <addr-line>Dept. of Chemistry and Biochemistry, 345 N. Campus Dr., Fayetteville, AR 72701.</addr-line>
Tel.: <phone>479-575-5607</phone>
; Fax: <fax>479-575-4049</fax>
; E-mail: <email>cheyes@uark.edu</email>
.</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>19</day>
<month>6</month>
<year>2015</year>
</pub-date>
<pub-date pub-type="epub"><day>27</day>
<month>4</month>
<year>2015</year>
</pub-date>
<volume>290</volume>
<issue>25</issue>
<fpage>15462</fpage>
<lpage>15474</lpage>
<history><date date-type="received"><day>7</day>
<month>11</month>
<year>2014</year>
</date>
<date date-type="rev-recd"><day>23</day>
<month>4</month>
<year>2015</year>
</date>
</history>
<permissions><copyright-statement>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
<copyright-year>2015</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc02515015462.pdf"></self-uri>
<abstract abstract-type="teaser"><p><bold>Background:</bold>
Targeting of proteins requires a signal recognition particle (SRP) and multiple protein interactions.</p>
<p><bold>Results:</bold>
We observed a decrease in the structural dynamics of cpSRP43 and an increase in substrate affinity upon its binding to cpSRP54.</p>
<p><bold>Conclusion:</bold>
Changes in domain dynamics induced by cpSRP subunit interactions mediate substrate affinity.</p>
<p><bold>Significance:</bold>
Relating structure and dynamics of SRP proteins allows for a better understanding of vectorial targeting within cells.</p>
</abstract>
<abstract><p>Protein targeting is critical in all living organisms and involves a signal recognition particle (SRP), an SRP receptor, and a translocase. In co-translational targeting, interactions among these proteins are mediated by the ribosome. In chloroplasts, the light-harvesting chlorophyll-binding protein (LHCP) in the thylakoid membrane is targeted post-translationally without a ribosome. A multidomain chloroplast-specific subunit of the SRP, cpSRP43, is proposed to take on the role of coordinating the sequence of targeting events. Here, we demonstrate that cpSRP43 exhibits significant interdomain dynamics that are reduced upon binding its SRP binding partner, cpSRP54. We showed that the affinity of cpSRP43 for the binding motif of LHCP (L18) increases when cpSRP43 is complexed to the binding motif of cpSRP54 (cpSRP54<sub>pep</sub>
). These results support the conclusion that substrate binding to the chloroplast SRP is modulated by protein structural dynamics in which a major role of cpSRP54 is to improve substrate binding efficiency to the cpSRP.</p>
</abstract>
<kwd-group><kwd>chloroplast</kwd>
<kwd>isothermal titration calorimetry (ITC)</kwd>
<kwd>membrane transport</kwd>
<kwd>molecular dynamics</kwd>
<kwd>protein dynamic</kwd>
<kwd>protein targeting</kwd>
<kwd>signal recognition particle (SRP)</kwd>
<kwd>single molecule biophysics</kwd>
</kwd-group>
<funding-group><award-group><funding-source id="CS100">National Institutes of Health</funding-source>
<award-id rid="CS100">P30 GM103450</award-id>
<award-id rid="CS100">1P30RR031154</award-id>
</award-group>
</funding-group>
</article-meta>
</front>
</pmc>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Ticri/CIDE/explor/CyberinfraV1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000042 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000042 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Ticri/CIDE |area= CyberinfraV1 |flux= Pmc |étape= Corpus |type= RBID |clé= |texte= }}
![]() | This area was generated with Dilib version V0.6.25. | ![]() |