Four distinct classes of proteins as interaction partners of the PABC domain of Arabidopsis thaliana Poly(A)-binding proteins
Identifieur interne : 002F94 ( Main/Exploration ); précédent : 002F93; suivant : 002F95Four distinct classes of proteins as interaction partners of the PABC domain of Arabidopsis thaliana Poly(A)-binding proteins
Auteurs : Jaime Bravo [Mexique] ; Laura Aguilar-Henonin [Mexique] ; Gabriela Olmedo [Mexique] ; Plinio Guzmán [Mexique]Source :
- Molecular Genetics and Genomics [ 1617-4615 ] ; 2005-02-01.
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Abstract
Abstract: Poly(A)-binding proteins (PABPs) play an important role in the regulation of translation and the control of mRNA stability in eukaryotes, and their functions are known to be essential in many organisms. PABPs contain a highly conserved C-terminal segment termed the PABC domain. The PABC domain from human PABP interacts with the proteins PAIP1, PAIP2 and RF3 via its PAM2 motifs. These interactions are important for modulating translation. Arabidopsis has eight PABPs, an unexpectedly large number in comparison to other eukaryotes whose genomes have been sequenced. Six of the Arabidopsis PABPs contain the conserved PABC domain. In this work, we have identified PABC-interacting proteins in Arabidopsis. Two proteins, which we named CID1 and CID7, were initially isolated in a two-hybrid screen, and eleven more were predicted to be present in the Arabidopsis proteome and eleven in the rice proteome. Among the 24 PAM2-containing proteins in this set, we observed a diversity of modules of intriguing function, ranging from acidic regions similar to the PAM1 motif found in human PAIP1 and PAIP2, to domains such as the small MutS-related domain, the Lsm domains of Ataxin-2, and RNA recognition motifs (RRMs). We suggest that the large number of PABPs and PAM2-containing proteins may have evolved to provide plants with greater flexibility in modulating the metabolism of specific transcripts. We also found that two PABP genes, PAB2 (ubiquitously expressed) and PAB5 (expressed in reproductive tissues), are essential for viability, suggesting that each has a vital and specific function.
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DOI: 10.1007/s00438-004-1090-9
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http://www.springer.de</publisher><pubPlace>Berlin/Heidelberg</pubPlace><date type="published" when="2005-02-01">2005-02-01</date><biblScope unit="volume">272</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="651">651</biblScope><biblScope unit="page" to="665">665</biblScope></imprint><idno type="ISSN">1617-4615</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1617-4615</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>PABC-interacting proteins</term><term>Post-transcriptional regulation</term><term>RNA-binding proteins</term><term>SMR motif</term><term>Yeast two-hybrid system</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Poly(A)-binding proteins (PABPs) play an important role in the regulation of translation and the control of mRNA stability in eukaryotes, and their functions are known to be essential in many organisms. PABPs contain a highly conserved C-terminal segment termed the PABC domain. The PABC domain from human PABP interacts with the proteins PAIP1, PAIP2 and RF3 via its PAM2 motifs. These interactions are important for modulating translation. Arabidopsis has eight PABPs, an unexpectedly large number in comparison to other eukaryotes whose genomes have been sequenced. Six of the Arabidopsis PABPs contain the conserved PABC domain. In this work, we have identified PABC-interacting proteins in Arabidopsis. Two proteins, which we named CID1 and CID7, were initially isolated in a two-hybrid screen, and eleven more were predicted to be present in the Arabidopsis proteome and eleven in the rice proteome. Among the 24 PAM2-containing proteins in this set, we observed a diversity of modules of intriguing function, ranging from acidic regions similar to the PAM1 motif found in human PAIP1 and PAIP2, to domains such as the small MutS-related domain, the Lsm domains of Ataxin-2, and RNA recognition motifs (RRMs). We suggest that the large number of PABPs and PAM2-containing proteins may have evolved to provide plants with greater flexibility in modulating the metabolism of specific transcripts. We also found that two PABP genes, PAB2 (ubiquitously expressed) and PAB5 (expressed in reproductive tissues), are essential for viability, suggesting that each has a vital and specific function.</div></front></TEI><affiliations><list><country><li>Mexique</li></country></list><tree><country name="Mexique"><noRegion><name sortKey="Bravo, Jaime" sort="Bravo, Jaime" uniqKey="Bravo J" first="Jaime" last="Bravo">Jaime Bravo</name></noRegion><name sortKey="Aguilar Henonin, Laura" sort="Aguilar Henonin, Laura" uniqKey="Aguilar Henonin L" first="Laura" last="Aguilar-Henonin">Laura Aguilar-Henonin</name><name sortKey="Guzman, Plinio" sort="Guzman, Plinio" uniqKey="Guzman P" first="Plinio" last="Guzmán">Plinio Guzmán</name><name sortKey="Guzman, Plinio" sort="Guzman, Plinio" uniqKey="Guzman P" first="Plinio" last="Guzmán">Plinio Guzmán</name><name sortKey="Olmedo, Gabriela" sort="Olmedo, Gabriela" uniqKey="Olmedo G" first="Gabriela" last="Olmedo">Gabriela Olmedo</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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