Quality control of the elongation step of protein synthesis by tmRNP

Citation
J. Wower et al., Quality control of the elongation step of protein synthesis by tmRNP, J NUTR, 131(11), 2001, pp. 2978S-2982S
Citations number
50
Categorie Soggetti
Food Science/Nutrition","Endocrinology, Nutrition & Metabolism
Journal title
JOURNAL OF NUTRITION
ISSN journal
00223166 → ACNP
Volume
131
Issue
11
Year of publication
2001
Pages
2978S - 2982S
Database
ISI
SICI code
0022-3166(200111)131:11<2978S:QCOTES>2.0.ZU;2-A
Abstract
Trans-translation is a quality-control process, activated upon premature te rmination of protein elongation, which recycles stalled ribosomes and degra des incomplete polypeptides. These functions are facilitated by transfer-me ssenger RNA (tmRNA, also called 10Sa RNA or SsrA RNA), a small stable RNA m olecule encoded by the SsrA gene found in bacteria, chloroplasts and mitoch ondria. Most tmRNAs consist of a tRNA- and an mRNA-like domain connected by up to four pseudoknots. Comparative sequence analysis provided the first i nsight into tmRNA secondary and three-dimensional structure. Studies of the E. coli tmRNA in vitro and in vivo demonstrated that tmRNA functions as a ribonucleoprotein (RNP) complex with elongation factor Tu (EF-Tu), protein SmpB and ribosomal protein S1. The tRNA-like and mRNA-like activities of tm RNA mark prematurely terminated proteins for degradation by attaching to th eir C-termini peptide tags, which are recognized by numerous proteases. Stu dies aimed at understanding the details of the molecular mechanisms of tran s-translation are ongoing.