Insights into the evolution and domain structure of ataxin-2 proteins across eukaryotes
Identifieur interne : 000A26 ( Main/Exploration ); précédent : 000A25; suivant : 000A27Insights into the evolution and domain structure of ataxin-2 proteins across eukaryotes
Auteurs : Domingo Jiménez-L Pez [Mexique] ; Plinio Guzmán [Mexique]Source :
- BMC Research Notes [ 1756-0500 ] ; 2014.
Abstract
Ataxin-2 is an evolutionarily conserved protein first identified in humans as responsible for spinocerebellar ataxia type 2 (SCA2). The molecular basis of SCA2 is the expansion of a polyglutamine tract in Ataxin-2, encoding a Lsm domain that may bind RNA and a PAM2 motif that enables interaction with the poly (A) binding protein. Although the association with SCA2 has been verified, a detailed molecular function for Ataxin-2 has not been established.
We have undertaken a survey of Ataxin-2 proteins across all eukaryotic domains. In eukaryotes, except for vertebrates and land plants, a single ortholog was identified. Notably, with the exception of birds, two Ataxin-2 genes exist in vertebrates. Expansion was observed in land plants and a novel class lacking the LsmAD domain was identified. Large polyQ tracts appear limited to primates and insects of the orders Hymenoptera and Diptera. A common feature across Ataxin-2 orthologs is the presence of proline-rich motifs, formerly described in the human protein.
Our analysis provides valuable information on the evolution and domain structure of Ataxin-2 proteins. Proline-rich motifs that may mediate protein interactions are widespread in Ataxin-2 proteins, but expansion of polyglutamine tracts associated with spinocerebellar ataxia type 2, is present only in primates, as well as some insects. Our analysis of Ataxin-2 proteins provides also a source to examine orthologs in a number of different species.
Url:
DOI: 10.1186/1756-0500-7-453
PubMed: 25027299
PubMed Central: 4105795
Affiliations:
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Le document en format XML
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<author><name sortKey="Jimenez L Pez, Domingo" sort="Jimenez L Pez, Domingo" uniqKey="Jimenez L Pez D" first="Domingo" last="Jiménez-L Pez">Domingo Jiménez-L Pez</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Insights into the evolution and domain structure of ataxin-2 proteins across eukaryotes</title>
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<author><name sortKey="Guzman, Plinio" sort="Guzman, Plinio" uniqKey="Guzman P" first="Plinio" last="Guzmán">Plinio Guzmán</name>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>Ataxin-2 is an evolutionarily conserved protein first identified in humans as responsible for spinocerebellar ataxia type 2 (SCA2). The molecular basis of SCA2 is the expansion of a polyglutamine tract in Ataxin-2, encoding a Lsm domain that may bind RNA and a PAM2 motif that enables interaction with the poly (A) binding protein. Although the association with SCA2 has been verified, a detailed molecular function for Ataxin-2 has not been established.</p>
</sec>
<sec><title>Results</title>
<p>We have undertaken a survey of Ataxin-2 proteins across all eukaryotic domains. In eukaryotes, except for vertebrates and land plants, a single ortholog was identified. Notably, with the exception of birds, two Ataxin-2 genes exist in vertebrates. Expansion was observed in land plants and a novel class lacking the LsmAD domain was identified. Large polyQ tracts appear limited to primates and insects of the orders Hymenoptera and Diptera. A common feature across Ataxin-2 orthologs is the presence of proline-rich motifs, formerly described in the human protein.</p>
</sec>
<sec><title>Conclusion</title>
<p>Our analysis provides valuable information on the evolution and domain structure of Ataxin-2 proteins. Proline-rich motifs that may mediate protein interactions are widespread in Ataxin-2 proteins, but expansion of polyglutamine tracts associated with spinocerebellar ataxia type 2, is present only in primates, as well as some insects. Our analysis of Ataxin-2 proteins provides also a source to examine orthologs in a number of different species.</p>
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