Document Detail

Characterization of Mycobacterium tuberculosis ribosome recycling factor (RRF) and a mutant lacking six amino acids from the C-terminal end reveals that the C-terminal residues are important for its occupancy on the ribosome.
MedLine Citation:
PMID:  12480895     Owner:  NLM     Status:  MEDLINE    
Ribosome recycling factor (RRF), coded for by the frr locus, is involved in the disassembly of post-termination complexes and recycling of the ribosomes for a fresh round of initiation in bacteria and in eukaryotic organelles. In a cross-species-complementation experiment, it was shown that the Thermus thermophilus RRF protein lacking five amino acids from its C-terminal end (deltaC5TthRRF) but not the full-length protein (TthRRF) complemented Escherichia coli for its frr(ts) phenotype. It was also shown that the Mycobacterium tuberculosis RFF protein (MtuRRF) did not complement E. coli LJ14 for frr(ts). However, simultaneous expression of elongation factor G (EFG) and RRF from M. tuberculosis resulted in complementation of E. coli LJ14. Here it is shown that unlike deltaC5TthRRF, an equivalent mutant of MtuRRF lacking six amino acids from its C-terminal end (deltaC6MtuRRF) did not complement E. coli LJ14. Surprisingly, deltaC6MtuRRF failed to complement the strain even in the presence of homologous EFG (MtuEFG). The biochemical and biophysical characterization of these proteins suggested that the mutant RRF folded properly. However, ribosome-binding assays showed that the mutant protein was compromised in its binding to E. coli ribosomes. It is suggested that the conserved amino acids at the C-terminal end of the RRFs contribute to their residency on ribosomes and that the specific interactions between RRF and EFG are crucial in the disassembly of the termination complex.
Arasada Rajeswara Rao; Umesh Varshney
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Microbiology (Reading, England)     Volume:  148     ISSN:  1350-0872     ISO Abbreviation:  Microbiology (Reading, Engl.)     Publication Date:  2002 Dec 
Date Detail:
Created Date:  2002-12-13     Completed Date:  2003-03-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9430468     Medline TA:  Microbiology     Country:  England    
Other Details:
Languages:  eng     Pagination:  3913-20     Citation Subset:  IM    
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560012, India.
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MeSH Terms
Amino Acid Sequence
Circular Dichroism
Escherichia coli / genetics,  metabolism
Genetic Complementation Test
Molecular Sequence Data
Mycobacterium tuberculosis / genetics*,  metabolism
Peptide Chain Termination, Translational / physiology
Peptide Elongation Factor G / genetics,  metabolism
Polyribosomes / metabolism
Proteins* / chemistry,  genetics,  isolation & purification,  metabolism
Ribosomal Proteins
Ribosomes / metabolism*
Sequence Alignment
Thermus thermophilus / genetics,  metabolism
Reg. No./Substance:
0/Peptide Elongation Factor G; 0/Proteins; 0/Ribosomal Proteins; 0/ribosome releasing factor

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