Novel function of C5 protein as a metabolic stabilizer of M1 RNA

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Escherichia coli RNase P is a ribonucleoprotein composed of a large RNA subunit (M1 RNA) and a small protein subunit (C5 protein). We examined if C5 protein plays a role in maintaining metabolic stability of M1 RNA. The sequestration of C5 protein available for M1 RNA binding reduced M1 RNA stability in vivo, and its reduced stability was recovered via overexpression of C5 protein. In addition, M1 RNA was rapidly degraded in a temperature-sensitive C5 protein mutant strain at non-permissive temperatures. Collectively, our results demonstrate that the C5 protein metabolically stabilizes M1 RNA in the cell. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2009-01
Language
English
Article Type
Article
Keywords

ESCHERICHIA-COLI RIBONUCLEASE; SITE-DIRECTED MUTAGENESIS; 4.5 S-RNA; GENE-EXPRESSION; MESSENGER-RNAS; ACCEPTOR STEM; P HOLOENZYME; CATALYSIS; PRECURSOR; SUBUNIT

Citation

FEBS LETTERS, v.583, no.2, pp.419 - 424

ISSN
0014-5793
DOI
10.1016/j.febslet.2008.12.040
URI
http://hdl.handle.net/10203/98800
Appears in Collection
CH-Journal Papers(저널논문)
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