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Trans ‐translation mediated by Bacillus subtilis tmRNA
Author(s) -
Ito Ken-ichi,
Tadaki Toshimasa,
Lee SungGa,
Takada Kazuma,
Muto Akira,
Himeno Hyouta
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02561-9
Subject(s) - bacillus subtilis , ribosome , escherichia coli , ef tu , biology , translation (biology) , peptide , microbiology and biotechnology , gene , messenger rna , biochemistry , chemistry , genetics , rna , bacteria
Trans ‐translation, in which a ribosome switches between translation of an mRNA and a tmRNA, produces a chimera polypeptide of an N‐terminal truncated polypeptide and a C‐terminal tag‐peptide encoded by tmRNA. One of the tmRNA binding proteins, a ribosomal protein S1, has not been found in a group of Gram‐positive bacteria. In this study, the trans ‐translation reaction with tmRNA from Bacillus subtilis belonging to this group was examined. When a truncated gene lacking a termination codon was expressed in B. subtilis , a 15‐amino acid tag‐peptide derived from tmRNA was identified in the C‐termini of the trans ‐translation products. An identical tag‐peptide was also found at the C‐termini of the products from a truncated gene, when it was coexpressed with B. subtilis tmRNA in Escherichia coli . B. subtilis tmRNA was functional, although much less efficiently, in the in vitro poly(U)‐dependent tag‐peptide synthesis system of E. coli . A comparison of two bacterial tmRNAs suggests that the rule for determining the tag‐initiation point on tmRNA may be the same in Gram‐positive and Gram‐negative bacteria.