PittsburghV1, Main, Exploration, bibRecord, 000218

Evolutionary and functional analysis of the invariant SWIM domain in the conserved Shu2/SWS1 protein family from Saccharomyces cerevisiae to Homo sapiens.

Identifieur interne : 000218 ( Main/Exploration ); précédent : 000217; suivant : 000219

Evolutionary and functional analysis of the invariant SWIM domain in the conserved Shu2/SWS1 protein family from Saccharomyces cerevisiae to Homo sapiens.

Auteurs : Stephen K. Godin [États-Unis] ; Camille Meslin-Auclair [États-Unis] ; Faiz Kabbinavar [États-Unis] ; Dominique S. Bratton-Palmer [États-Unis] ; Christina Hornack [États-Unis] ; Michael J. Mihalevic [États-Unis] ; Kyle Yoshida [États-Unis] ; Meghan Sullivan [États-Unis] ; Nathan L. Clark [États-Unis] ; Kara A. Bernstein [États-Unis]

Source :

Genetics [ 0016-6731 ] ; 2015.

RBID : Hal:hal-01606531

English descriptors

mix :
- DNA repair, Shu complex, budding yeast, evolutionary rate covariation, homologous recombination.

Abstract

The Saccharomyces cerevisiae Shu2 protein is an important regulator of Rad51, which promotes homologous recombination (HR). Shu2 functions in the Shu complex with Shu1 and the Rad51 paralogs Csm2 and Psy3. Shu2 belongs to the SWS1 protein family, which is characterized by its SWIM domain (CXC...Xn...CXH), a zinc-binding motif. In humans, SWS1 interacts with the Rad51 paralog SWSAP1. Using genetic and evolutionary analyses, we examined the role of the Shu complex in mitotic and meiotic processes across eukaryotic lineages. We provide evidence that the SWS1 protein family contains orthologous genes in early-branching eukaryote lineages (e.g., Giardia lamblia), as well as in multicellular eukaryotes including Caenorhabditis elegans and Drosophila melanogaster. Using sequence analysis, we expanded the SWIM domain to include an invariant alanine three residues after the terminal CXH motif (CXC…Xn…CXHXXA). We found that the SWIM domain is conserved in all eukaryotic orthologs, and accordingly, in vivo disruption of the invariant residues within the canonical SWIM domain inhibits DNA damage tolerance in yeast and protein-protein interactions in yeast and humans. Furthermore, using evolutionary analyses, we found that yeast and Drosophila Shu2 exhibit strong coevolutionary signatures with meiotic proteins, and in yeast, its disruption leads to decreased meiotic progeny. Together our data indicate that the SWS1 family is an ancient and highly conserved eukaryotic regulator of meiotic and mitotic HR.

Url:

https://hal.archives-ouvertes.fr/hal-01606531

DOI: 10.1534/genetics.114.173518

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Hal, to step Corpus: 000264
to stream Hal, to step Curation: 000264
to stream Hal, to step Checkpoint: 000183
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to stream Main, to step Curation: 000218

Le document en format XML

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<author><name sortKey="Clark, Nathan L" sort="Clark, Nathan L" uniqKey="Clark N" first="Nathan L" last="Clark">Nathan L. Clark</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-515916" status="INCOMING">          <orgName>School of Medicine, Department of Computational and Systems Biology</orgName>
          <desc>            <address>              <country key="US"></country>
            </address>
          </desc>
          <listRelation>            <relation active="#struct-418259" type="direct"></relation>
          </listRelation>
        <tutelles><tutelle active="#struct-418259" type="direct"><org type="institution" xml:id="struct-418259" status="INCOMING">          <orgName>University of Pittsburgh</orgName>
          <desc>            <address>              <country key="US"></country>
            </address>
          </desc>
        </org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>États-Unis</country>
<placeName><settlement type="city">Pittsburgh</settlement>
<region type="state">Pennsylvanie</region>
</placeName>
<orgName type="university">Université de Pittsburgh</orgName>
</affiliation>
</author>
<author><name sortKey="Bernstein, Kara A" sort="Bernstein, Kara A" uniqKey="Bernstein K" first="Kara A" last="Bernstein">Kara A. Bernstein</name>
<affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-515915" status="INCOMING">          <orgName>Cancer Institute and Department of Microbiology and Molecular Genetics</orgName>
          <desc>            <address>              <country key="US"></country>
            </address>
          </desc>
          <listRelation>            <relation active="#struct-418259" type="direct"></relation>
          </listRelation>
        <tutelles><tutelle active="#struct-418259" type="direct"><org type="institution" xml:id="struct-418259" status="INCOMING">          <orgName>University of Pittsburgh</orgName>
          <desc>            <address>              <country key="US"></country>
            </address>
          </desc>
        </org>
</tutelle>
</tutelles>
</hal:affiliation>
<country>États-Unis</country>
<placeName><settlement type="city">Pittsburgh</settlement>
<region type="state">Pennsylvanie</region>
</placeName>
<orgName type="university">Université de Pittsburgh</orgName>
</affiliation>
</author>
</analytic>
<idno type="DOI">10.1534/genetics.114.173518</idno>
<series><title level="j">Genetics</title>
<idno type="ISSN">0016-6731</idno>
<imprint><date type="datePub">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>DNA repair</term>
<term>Shu complex</term>
<term>budding yeast</term>
<term>evolutionary rate covariation</term>
<term>homologous recombination</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The Saccharomyces cerevisiae Shu2 protein is an important regulator of Rad51, which promotes homologous recombination (HR). Shu2 functions in the Shu complex with Shu1 and the Rad51 paralogs Csm2 and Psy3. Shu2 belongs to the SWS1 protein family, which is characterized by its SWIM domain (CXC...Xn...CXH), a zinc-binding motif. In humans, SWS1 interacts with the Rad51 paralog SWSAP1. Using genetic and evolutionary analyses, we examined the role of the Shu complex in mitotic and meiotic processes across eukaryotic lineages. We provide evidence that the SWS1 protein family contains orthologous genes in early-branching eukaryote lineages (e.g., Giardia lamblia), as well as in multicellular eukaryotes including Caenorhabditis elegans and Drosophila melanogaster. Using sequence analysis, we expanded the SWIM domain to include an invariant alanine three residues after the terminal CXH motif (CXC…Xn…CXHXXA). We found that the SWIM domain is conserved in all eukaryotic orthologs, and accordingly, in vivo disruption of the invariant residues within the canonical SWIM domain inhibits DNA damage tolerance in yeast and protein-protein interactions in yeast and humans. Furthermore, using evolutionary analyses, we found that yeast and Drosophila Shu2 exhibit strong coevolutionary signatures with meiotic proteins, and in yeast, its disruption leads to decreased meiotic progeny. Together our data indicate that the SWS1 family is an ancient and highly conserved eukaryotic regulator of meiotic and mitotic HR.</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Pennsylvanie</li>
</region>
<settlement><li>Pittsburgh</li>
</settlement>
<orgName><li>Université de Pittsburgh</li>
</orgName>
</list>
<tree><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Godin, Stephen K" sort="Godin, Stephen K" uniqKey="Godin S" first="Stephen K" last="Godin">Stephen K. Godin</name>
</region>
<name sortKey="Bernstein, Kara A" sort="Bernstein, Kara A" uniqKey="Bernstein K" first="Kara A" last="Bernstein">Kara A. Bernstein</name>
<name sortKey="Bratton Palmer, Dominique S" sort="Bratton Palmer, Dominique S" uniqKey="Bratton Palmer D" first="Dominique S" last="Bratton-Palmer">Dominique S. Bratton-Palmer</name>
<name sortKey="Clark, Nathan L" sort="Clark, Nathan L" uniqKey="Clark N" first="Nathan L" last="Clark">Nathan L. Clark</name>
<name sortKey="Hornack, Christina" sort="Hornack, Christina" uniqKey="Hornack C" first="Christina" last="Hornack">Christina Hornack</name>
<name sortKey="Kabbinavar, Faiz" sort="Kabbinavar, Faiz" uniqKey="Kabbinavar F" first="Faiz" last="Kabbinavar">Faiz Kabbinavar</name>
<name sortKey="Meslin Auclair, Camille" sort="Meslin Auclair, Camille" uniqKey="Meslin Auclair C" first="Camille" last="Meslin-Auclair">Camille Meslin-Auclair</name>
<name sortKey="Mihalevic, Michael J" sort="Mihalevic, Michael J" uniqKey="Mihalevic M" first="Michael J" last="Mihalevic">Michael J. Mihalevic</name>
<name sortKey="Sullivan, Meghan" sort="Sullivan, Meghan" uniqKey="Sullivan M" first="Meghan" last="Sullivan">Meghan Sullivan</name>
<name sortKey="Yoshida, Kyle" sort="Yoshida, Kyle" uniqKey="Yoshida K" first="Kyle" last="Yoshida">Kyle Yoshida</name>
</country>
</tree>
</affiliations>
</record>

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Evolutionary and functional analysis of the invariant SWIM domain in the conserved Shu2/SWS1 protein family from Saccharomyces cerevisiae to Homo sapiens.

Evolutionary and functional analysis of the invariant SWIM domain in the conserved Shu2/SWS1 protein family from Saccharomyces cerevisiae to Homo sapiens.

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