2hx6
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(New page: 200px<br /><applet load="2hx6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hx6" /> '''Solution structure analysis of the phage T4 ...)
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Revision as of 09:54, 21 November 2007
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Solution structure analysis of the phage T4 endoribonuclease RegB
Overview
The RegB endoribonuclease participates in the bacteriophage T4 life cycle, by favoring early messenger RNA breakdown. RegB specifically cleaves GGAG, sequences found in intergenic regions, mainly in translation initiation, sites. Its activity is very low but can be enhanced up to 100-fold by the, ribosomal 30 S subunit or by ribosomal protein S1. RegB has no significant, sequence homology to any known protein. Here we used NMR to solve the, structure of RegB and map its interactions with two RNA substrates. We, also generated a collection of mutants affected in RegB function. Our, results show that, despite the absence of any sequence homology, RegB has, structural similarities with two Escherichia coli ribonucleases involved, in mRNA inactivation on translating ribosomes: YoeB and RelE. Although, these ribonucleases have different catalytic sites, we propose that RegB, is a new member of the RelE/YoeB structural and functional family of, ribonucleases specialized in mRNA inactivation within the ribosome.
About this Structure
2HX6 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome., Odaert B, Saida F, Aliprandi P, Durand S, Crechet JB, Guerois R, Laalami S, Uzan M, Bontems F, J Biol Chem. 2007 Jan 19;282(3):2019-28. Epub 2006 Oct 17. PMID:17046813
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