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Science 26 May 1995:
Vol. 268. no. 5214, pp. 1170 - 1173
DOI: 10.1126/science.7761833

Articles

Science, Vol 268, Issue 5214, 1170-1173
Copyright © 1995 by American Association for the Advancement of Science


articles

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

C Kang, R Chan, I Berger, C Lockshin, L Green, L Gold, and A Rich

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
RegA proteins from phage T4 and RB69 have conserved helix-loop groove RNA binding motifs but different RNA binding specificities.
T. K. Sengupta, J. Gordon, and E. K. Spicer (2001)
Nucleic Acids Res. 29, 1175-1184
   Abstract »    Full Text »    PDF »
Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis.
J. Gordon, T. K. Sengupta, C. A. Phillips, S. M. O'Malley, K. R. Williams, and E. K. Spicer (1999)
J. Biol. Chem. 274, 32265-32273
   Abstract »    Full Text »    PDF »
Single-stranded RNA Recognition by the Bacteriophage T4 Translational Repressor, RegA.
D. Brown, J. Brown, C. Kang, L. Gold, and P. Allen (1997)
J. Biol. Chem. 272, 14969-14974
   Abstract »    Full Text »    PDF »
From oligonucleotide shapes to genomic SELEX: Novel biological regulatory loops.
L. Gold, D. Brown, Y.-y. He, T. Shtatland, B. S. Singer, and Y. Wu (1997)
PNAS 94, 59-64
   Abstract »    Full Text »    PDF »



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