Four distinct classes of proteins as interaction partners of the PABC domain of Arabidopsis thaliana Poly(A)-binding proteins

作者: Jaime Bravo , Laura Aguilar-Henonin , Gabriela Olmedo , Plinio Guzmán

DOI: 10.1007/S00438-004-1090-9

关键词:

摘要: Poly(A)-binding proteins (PABPs) play an important role in the regulation of translation and control mRNA stability eukaryotes, their functions are known to be essential many organisms. PABPs contain a highly conserved C-terminal segment termed PABC domain. The domain from human PABP interacts with PAIP1, PAIP2 RF3 via its PAM2 motifs. These interactions for modulating translation. Arabidopsis has eight PABPs, unexpectedly large number comparison other eukaryotes whose genomes have been sequenced. Six In this work, we identified PABC-interacting Arabidopsis. Two proteins, which named CID1 CID7, were initially isolated two-hybrid screen, eleven more predicted present proteome rice proteome. Among 24 PAM2-containing set, observed diversity modules intriguing function, ranging acidic regions similar PAM1 motif found PAIP1 PAIP2, domains such as small MutS-related domain, Lsm Ataxin-2, RNA recognition motifs (RRMs). We suggest that may evolved provide plants greater flexibility metabolism specific transcripts. also two genes, PAB2 (ubiquitously expressed) PAB5 (expressed reproductive tissues), viability, suggesting each vital function.

参考文章(55)
Valérie Hecht, Virginia Stiefel, Michel Delseny, Patrick Gallois, A new Arabidopsis nucleic-acid-binding protein gene is highly expressed in dividing cells during development Plant Molecular Biology. ,vol. 34, pp. 119- 124 ,(1997) , 10.1023/A:1005834402536
Hosoda N, Hoshino S, Uchida N, Katada T, Araki Y, Funakoshi Y, Kobayashi T, Novel function of the eukaryotic polypeptide-chain releasing factor 3 (eRF3/GSPT) in the mRNA degradation pathway. Biochemistry. ,vol. 64, pp. 1367- ,(1999)
Mario Albrecht, Michael Golatta, Ullrich Wüllner, Thomas Lengauer, Structural and functional analysis of ataxin-2 and ataxin-3. FEBS Journal. ,vol. 271, pp. 3155- 3170 ,(2004) , 10.1111/J.1432-1033.2004.04245.X
Stephan J. Sigrist, Philippe R. Thiel, Dierk F. Reiff, Pascal E. D. Lachance, Paul Lasko, Christoph M. Schuster, Postsynaptic translation affects the efficacy and morphology of neuromuscular junctions Nature. ,vol. 405, pp. 1062- 1065 ,(2000) , 10.1038/35016598
Andrew W. B. Craig, Ashkan Haghighat, Annie T. K. Yu, Nahum Sonenberg, Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation Nature. ,vol. 392, pp. 520- 523 ,(1998) , 10.1038/33198
N Amrani, M Minet, M Le Gouar, F Lacroute, F Wyers, Yeast Pab1 Interacts with Rna15 and Participates in the Control of the Poly(A) Tail Length In Vitro Molecular and Cellular Biology. ,vol. 17, pp. 3694- 3701 ,(1997) , 10.1128/MCB.17.7.3694
A B Sachs, R W Davis, R D Kornberg, A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability Molecular and Cellular Biology. ,vol. 7, pp. 3268- 3276 ,(1987) , 10.1128/MCB.7.9.3268