SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon
Abo, T; Inada, T; Ogawa, K; Aiba, H
| HERO ID | 1617050 |
|---|---|
| In Press | No |
| Year | 2000 |
| Title | SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon |
| Authors | Abo, T; Inada, T; Ogawa, K; Aiba, H |
| Journal | EMBO Journal |
| Volume | 19 |
| Issue | 14 |
| Page Numbers | 3762-3769 |
| Abstract | SsrA RNA of Escherichia coli, also known as 10Sa RNA or tmRNA, acts both as tRNA and mRNA when ribosomes are paused at the 3' end of an mRNA lacking a stop codon. This process, referred to as trans-translation, leads to the addition of a short peptide tag to the C-terminus of the incomplete nascent polypeptide. The tagged polypeptide is then degraded by C-terminal-specific proteases. Here, we focused on endogenous targets for the SsrA system and on a potential regulatory role of SsrA RNA. First, we show that trans-translation events occur frequently in normally growing E. COLI: cells. More specifically, we report that the lacI mRNA encoding Lac repressor (LacI) is a specific natural target for trans-translation. The binding of LacI to the lac operators results in truncated lacI mRNAs that are, in turn, recognized by the SsrA system. The SsrA-mediated tagging and proteolysis of LacI appears to play a role in cellular adaptation to lactose availability by supporting a rapid induction of lac operon expression. |
| Doi | 10.1093/emboj/19.14.3762 |
| Pmid | 10899129 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |