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Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates*

Identifieur interne : 000072 ( Pmc/Checkpoint ); précédent : 000071; suivant : 000073

Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates*

Auteurs : Feng Gao ; Alicia D. Kight [États-Unis] ; Rory Henderson ; Srinivas Jayanthi ; Parth Patel ; Marissa Murchison ; Priyanka Sharma [États-Unis] ; Robyn L. Goforth [États-Unis] ; Thallapuranam Krishnaswamy Suresh Kumar ; Ralph L. Henry [États-Unis] ; Colin D. Heyes

Source :

RBID : PMC:4505461

Abstract

Background: Targeting of proteins requires a signal recognition particle (SRP) and multiple protein interactions.

Results: We observed a decrease in the structural dynamics of cpSRP43 and an increase in substrate affinity upon its binding to cpSRP54.

Conclusion: Changes in domain dynamics induced by cpSRP subunit interactions mediate substrate affinity.

Significance: Relating structure and dynamics of SRP proteins allows for a better understanding of vectorial targeting within cells.


Url:
DOI: 10.1074/jbc.M114.624346
PubMed: 25918165
PubMed Central: 4505461


Affiliations:


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PMC:4505461

Le document en format XML

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<author>
<name sortKey="Jayanthi, Srinivas" sort="Jayanthi, Srinivas" uniqKey="Jayanthi S" first="Srinivas" last="Jayanthi">Srinivas Jayanthi</name>
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<nlm:aff id="aff1"></nlm:aff>
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<country xml:lang="fr">États-Unis</country>
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<affiliation wicri:level="2">
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<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">Arkansas</region>
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<wicri:cityArea>Biological Sciences, University of Arkansas, Fayetteville</wicri:cityArea>
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<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>
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<name sortKey="Henry, Ralph L" sort="Henry, Ralph L" uniqKey="Henry R" first="Ralph L." last="Henry">Ralph L. Henry</name>
<affiliation wicri:level="2">
<nlm:aff id="aff2">Biological Sciences, University of Arkansas, Fayetteville, Arkansas 72701</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">Arkansas</region>
</placeName>
<wicri:cityArea>Biological Sciences, University of Arkansas, Fayetteville</wicri:cityArea>
</affiliation>
</author>
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<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>
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<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>
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<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>
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<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>
<affiliations>
<list>
<country>
<li>États-Unis</li>
</country>
<region>
<li>Arkansas</li>
</region>
</list>
<tree>
<noCountry>
<name sortKey="Gao, Feng" sort="Gao, Feng" uniqKey="Gao F" first="Feng" last="Gao">Feng Gao</name>
<name sortKey="Henderson, Rory" sort="Henderson, Rory" uniqKey="Henderson R" first="Rory" last="Henderson">Rory Henderson</name>
<name sortKey="Heyes, Colin D" sort="Heyes, Colin D" uniqKey="Heyes C" first="Colin D." last="Heyes">Colin D. Heyes</name>
<name sortKey="Jayanthi, Srinivas" sort="Jayanthi, Srinivas" uniqKey="Jayanthi S" first="Srinivas" last="Jayanthi">Srinivas Jayanthi</name>
<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>
<name sortKey="Murchison, Marissa" sort="Murchison, Marissa" uniqKey="Murchison M" first="Marissa" last="Murchison">Marissa Murchison</name>
<name sortKey="Patel, Parth" sort="Patel, Parth" uniqKey="Patel P" first="Parth" last="Patel">Parth Patel</name>
</noCountry>
<country name="États-Unis">
<region name="Arkansas">
<name sortKey="Kight, Alicia D" sort="Kight, Alicia D" uniqKey="Kight A" first="Alicia D." last="Kight">Alicia D. Kight</name>
</region>
<name sortKey="Goforth, Robyn L" sort="Goforth, Robyn L" uniqKey="Goforth R" first="Robyn L." last="Goforth">Robyn L. Goforth</name>
<name sortKey="Henry, Ralph L" sort="Henry, Ralph L" uniqKey="Henry R" first="Ralph L." last="Henry">Ralph L. Henry</name>
<name sortKey="Sharma, Priyanka" sort="Sharma, Priyanka" uniqKey="Sharma P" first="Priyanka" last="Sharma">Priyanka Sharma</name>
</country>
</tree>
</affiliations>
</record>

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}}

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HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Checkpoint/RBID.i   -Sk "pubmed:25918165" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a CyberinfraV1 

Wicri

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Data generation: Thu Oct 27 09:30:58 2016. Site generation: Sun Mar 10 23:08:40 2024