Literature DB >> 7761833

Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution.

C Kang1, R Chan, I Berger, C Lockshin, L Green, L Gold, A Rich.   

Abstract

The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction.

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Year:  1995        PMID: 7761833     DOI: 10.1126/science.7761833

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  9 in total

1.  Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains.

Authors:  Alexey Teplyakov; Galina Obmolova; Nivedita Bir; Prasad Reddy; Andrew J Howard; Gary L Gilliland
Journal:  J Struct Funct Genomics       Date:  2003

Review 2.  Overview of protein structural and functional folds.

Authors:  Peter D Sun; Christine E Foster; Jeffrey C Boyington
Journal:  Curr Protoc Protein Sci       Date:  2004-05

3.  Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.

Authors:  S Nikonov; N Nevskaya; I Eliseikina; N Fomenkova; A Nikulin; N Ossina; M Garber; B H Jonsson; C Briand; S Al-Karadaghi; A Svensson; A Aevarsson; A Liljas
Journal:  EMBO J       Date:  1996-03-15       Impact factor: 11.598

4.  Bacteriophage T4 regA protein binds RNA as a monomer, overcoming dimer interactions.

Authors:  C A Phillips; J Gordon; E K Spicer
Journal:  Nucleic Acids Res       Date:  1996-11-01       Impact factor: 16.971

5.  From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins.

Authors:  X Manival; Y Yang; M P Strub; M Kochoyan; M Steinmetz; S Aymerich
Journal:  EMBO J       Date:  1997-08-15       Impact factor: 11.598

6.  RegA proteins from phage T4 and RB69 have conserved helix-loop groove RNA binding motifs but different RNA binding specificities.

Authors:  T K Sengupta; J Gordon; E K Spicer
Journal:  Nucleic Acids Res       Date:  2001-03-01       Impact factor: 16.971

Review 7.  From oligonucleotide shapes to genomic SELEX: novel biological regulatory loops.

Authors:  L Gold; D Brown; Y He; T Shtatland; B S Singer; Y Wu
Journal:  Proc Natl Acad Sci U S A       Date:  1997-01-07       Impact factor: 11.205

8.  Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein.

Authors:  M Huenges; C Rölz; R Gschwind; R Peteranderl; F Berglechner; G Richter; A Bacher; H Kessler; G Gemmecker
Journal:  EMBO J       Date:  1998-07-15       Impact factor: 11.598

Review 9.  Post-transcriptional control by bacteriophage T4: mRNA decay and inhibition of translation initiation.

Authors:  Marc Uzan; Eric S Miller
Journal:  Virol J       Date:  2010-12-03       Impact factor: 4.099

  9 in total

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