Authors: Hirokawa, Go; Inokuchi, Hachiro¹; Kaji, Hideko²; Igarashi, Kazuei³; Kaji, Akira⁴

Source: Molecular Microbiology, Volume 54, Number 4, November 2004 , pp. 1011-1021(11)

Publisher: Wiley-Blackwell

Abstract:

Summary

The post-termination ribosomal complex is disassembled by ribosome recycling factor (RRF) and elongation factor G. Without RRF, the ribosome is not released from mRNA at the termination codon and reinitiates translation downstream. This is called unscheduled translation. Here, we show that at the non-permissive temperature of a temperature-sensitive RRF strain, RRF is lost quickly, and some ribosomes reach the 3′ end of mRNA. However, instead of accumulating at the 3′ end of mRNA, ribosomes are released as monosomes. Some ribosomes are transferred to transfer-messenger RNA from the 3′ end of mRNA. The monosomes thus produced are able to translate synthetic homopolymer but not natural mRNA with leader and canonical initiation signal. The pellet containing ribosomes appears to be responsible for rapid but reversible inhibition of most but not all of protein synthesis in vivo closely followed by decrease of cellular RNA and DNA synthesis.

Document Type: Research article

DOI: http://dx.doi.org/10.1111/j.1365-2958.2004.04324.x

Affiliations: 1: Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan. 2: Department of Biochemistry and Molecular Pharmacology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, PA 19107, USA. 3: Department of Clinical Biochemistry, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba 260-8675, Japan. 4: Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Publication date: 2004-11-01

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