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In vivo effect of inactivation of ribosome recycling factor – fate of ribosomes after unscheduled translation downstream of open reading frame
Author(s) -
Hirokawa Go,
Inokuchi Hachiro,
Kaji Hideko,
Igarashi Kazuei,
Kaji Akira
Publication year - 2004
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2004.04324.x
Subject(s) - ribosome , biology , messenger rna , translation (biology) , protein biosynthesis , open reading frame , rna , microbiology and biotechnology , internal ribosome entry site , translational frameshift , transfer rna , biochemistry , gene , peptide sequence
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.