Novel function of C5 protein as a metabolic stabilizer of M1 RNA.
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.
Kim
Yool
Y
Department of Chemistry, KAIST, Daejeon 305-701, Republic of Korea.
Lee
Younghoon
Y
D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009690:Nucleic Acid Conformation; D021122:Protein Subunits / Q000378:metabolism; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D020871:RNA Stability; D043262:Ribonuclease P / Q000235:genetics / Q000378:metabolism*
D029968:Escherichia coli Proteins; D021122:Protein Subunits; D012313:RNA; D043262:Ribonuclease P; C470865:ribonuclease P, E coli