Literature DB >> 1383091

Translational initiation factors IF-1 and eIF-2 alpha share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase.

M Gribskov1.   

Abstract

Initiation of translation is a complicated process involving numerous accessory factors whose functions remain incompletely understood. Bacterial ribosomal protein S1 is known to contain a repeated sequence motif (S1-RM), also found in polynucleotide phosphorylase, that is thought to be involved in binding to RNA. Using the technique of profile analysis, the S1-RM can also be found in bacterial and chloroplast translation initiation factor IF-1 sequences, and in the sequences of eukaryotic translation initiation factor eIF-2 alpha chains. The significance of the similarity of the sequences is very high suggesting that the occurrence of the S1-RM in these diverse proteins represents homology. The similarity of S1 to IF-1 further suggests that S1 has evolved from an IF-1 like ancestor, and therefore that the two proteins have a similar or competitive function. The most obvious common function of the proteins containing the S1-RM seems to be RNA binding, suggesting that IF-1 and eIF-2 alpha may bind to RNA.

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Year:  1992        PMID: 1383091     DOI: 10.1016/0378-1119(92)90073-x

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  21 in total

1.  Genome analysis: Assigning protein coding regions to three-dimensional structures.

Authors:  A A Salamov; M Suwa; C A Orengo; M B Swindells
Journal:  Protein Sci       Date:  1999-04       Impact factor: 6.725

2.  Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA.

Authors:  J Sengupta; R K Agrawal; J Frank
Journal:  Proc Natl Acad Sci U S A       Date:  2001-10-02       Impact factor: 11.205

Review 3.  Origin and evolution of the ribosome.

Authors:  George E Fox
Journal:  Cold Spring Harb Perspect Biol       Date:  2010-06-09       Impact factor: 10.005

4.  An RNA Chaperone-Like Protein Plays Critical Roles in Chloroplast mRNA Stability and Translation in Arabidopsis and Maize.

Authors:  Jingjing Jiang; Xin Chai; Nikolay Manavski; Rosalind Williams-Carrier; Baoye He; Andreas Brachmann; Daili Ji; Min Ouyang; Yini Liu; Alice Barkan; Jörg Meurer; Lixin Zhang; Wei Chi
Journal:  Plant Cell       Date:  2019-04-08       Impact factor: 11.277

5.  Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation.

Authors:  T Krishnamoorthy; G D Pavitt; F Zhang; T E Dever; A G Hinnebusch
Journal:  Mol Cell Biol       Date:  2001-08       Impact factor: 4.272

6.  Computational learning reveals coiled coil-like motifs in histidine kinase linker domains.

Authors:  M Singh; B Berger; P S Kim; J M Berger; A G Cochran
Journal:  Proc Natl Acad Sci U S A       Date:  1998-03-17       Impact factor: 11.205

7.  Specific binding of Escherichia coli ribosomal protein S1 to boxA transcriptional antiterminator RNA.

Authors:  J Mogridge; J Greenblatt
Journal:  J Bacteriol       Date:  1998-04       Impact factor: 3.490

8.  Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome: identification of a novel S1 domain-containing protein and unusually large orthologs of bacterial S2, S3, and S5.

Authors:  Kenichi Yamaguchi; Susana Prieto; María Verónica Beligni; Paul A Haynes; W Hayes McDonald; John R Yates; Stephen P Mayfield
Journal:  Plant Cell       Date:  2002-11       Impact factor: 11.277

9.  Ribosomal protein S1 functions as a termination factor in RNA synthesis by Qβ phage replicase.

Authors:  Nikita N Vasilyev; Zarina S Kutlubaeva; Victor I Ugarov; Helena V Chetverina; Alexander B Chetverin
Journal:  Nat Commun       Date:  2013       Impact factor: 14.919

10.  GTPases and the origin of the ribosome.

Authors:  Hyman Hartman; Temple F Smith
Journal:  Biol Direct       Date:  2010-05-20       Impact factor: 4.540

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