| Structural highlights
Function
[RRAA_ECOLI] Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing in vivo and in vitro. Here, we report the 2.0A X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12A in diameter. Based on earlier sequence analysis, RraA had been identified as a putative S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the E.coli RraA exhibits an ancient relationship to a family of aldolases.
The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing.,Monzingo AF, Gao J, Qiu J, Georgiou G, Robertus JD J Mol Biol. 2003 Oct 3;332(5):1015-24. PMID:14499605[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee K, Zhan X, Gao J, Qiu J, Feng Y, Meganathan R, Cohen SN, Georgiou G. RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell. 2003 Sep 5;114(5):623-34. PMID:13678585
- ↑ Yeom JH, Lee K. RraA rescues Escherichia coli cells over-producing RNase E from growth arrest by modulating the ribonucleolytic activity. Biochem Biophys Res Commun. 2006 Jul 14;345(4):1372-6. Epub 2006 May 11. PMID:16725107 doi:10.1016/j.bbrc.2006.05.018
- ↑ Gao J, Lee K, Zhao M, Qiu J, Zhan X, Saxena A, Moore CJ, Cohen SN, Georgiou G. Differential modulation of E. coli mRNA abundance by inhibitory proteins that alter the composition of the degradosome. Mol Microbiol. 2006 Jul;61(2):394-406. Epub 2006 Jun 12. PMID:16771842 doi:10.1111/j.1365-2958.2006.05246.x
- ↑ Yeom JH, Go H, Shin E, Kim HL, Han SH, Moore CJ, Bae J, Lee K. Inhibitory effects of RraA and RraB on RNAse E-related enzymes imply conserved functions in the regulated enzymatic cleavage of RNA. FEMS Microbiol Lett. 2008 Aug;285(1):10-5. doi: 10.1111/j.1574-6968.2008.01205.x., Epub 2008 May 28. PMID:18510556 doi:10.1111/j.1574-6968.2008.01205.x
- ↑ Gorna MW, Pietras Z, Tsai YC, Callaghan AJ, Hernandez H, Robinson CV, Luisi BF. The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome. RNA. 2010 Jan 27. PMID:20106955 doi:rna.1858010
- ↑ Monzingo AF, Gao J, Qiu J, Georgiou G, Robertus JD. The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing. J Mol Biol. 2003 Oct 3;332(5):1015-24. PMID:14499605
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