PMID: 9537394Apr 16, 1998Paper

Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay

Journal of Bacteriology
R F WangS R Kushner

Abstract

The mrsC gene of Escherichia coli is required for mRNA turnover and cell growth, and strains containing the temperature-sensitive mrsC505 allele have longer half-lives than wild-type controls for total pulse-labeled and individual mRNAs (L. L. Granger et al., J. Bacteriol. 180:1920-1928, 1998). The cloned mrsC gene contains a long open reading frame beginning at an initiator UUG codon, confirmed by N-terminal amino acid sequencing, encoding a 70,996-Da protein with a consensus ATP-binding domain. mrsC is identical to the independently identified ftsH gene except for three additional amino acids at the N terminus (T. Tomoyasu et al., J. Bacteriol. 175:1344-1351, 1993). The purified protein had a Km of 28 microM for ATP and a Vmax of 21.2 nmol/microg/min. An amino-terminal glutathione S-transferase-MrsC fusion protein retained ATPase activity but was not biologically active. A glutamic acid replacement of the highly conserved lysine within the ATP-binding motif (mrsC201) abolished the complementation of the mrsC505 mutation, confirming that the ATPase activity is required for MrsC function in vivo. In addition, the mrsC505 allele conferred a temperature-sensitive HflB phenotype, while the hflB29 mutation promoted mRNA stability a...Continue Reading

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Citations

Mar 26, 2016·DNA Research : an International Journal for Rapid Publication of Reports on Genes and Genomes·Kenji NakahigashiHirotada Mori
Feb 13, 1999·Molecular Microbiology·M Carmona, V de Lorenzo
Mar 17, 1999·FEMS Microbiology Reviews·W Schumann
May 25, 2005·Annual Review of Microbiology·Koreaki Ito, Yoshinori Akiyama
Jun 17, 1999·FEMS Microbiology Reviews·A W Nicholson
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Apr 16, 1998·Journal of Bacteriology·L L GrangerS R Kushner
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May 14, 1999·Current Opinion in Microbiology·S Gottesman
Apr 1, 2007·EcoSal Plus·Sidney R Kushner
Sep 8, 1998·Microbiology and Molecular Biology Reviews : MMBR·M K Berlyn

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