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Nucleic Acids Research 2005 33(17):5591-5601; doi:10.1093/nar/gki864
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Published online 30 September 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
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Article

Evidence for a role of initiation factor 3 in recycling of ribosomal complexes stalled on mRNAs in Escherichia coli

N. S. Singh, G. Das, A. Seshadri, R. Sangeetha and U. Varshney*

Department of Microbiology and Cell Biology, Indian Institute of Science Bangalore 560012, India

*To whom correspondence should be addressed. Tel: +91 80 2293 2686; Fax: +91 80 2360 2697; Email: varshney{at}mcbl.iisc.ernet.in

Received August 17, 2005. Revised September 8, 2005. Accepted September 8, 2005.

Specific interactions between ribosome recycling factor (RRF) and elongation factor-G (EFG) mediate disassembly of post-termination ribosomal complexes for new rounds of initiation. The interactions between RRF and EFG are also important in peptidyl-tRNA release from stalled pre-termination complexes. Unlike the post-termination complexes (harboring deacylated tRNA), the pre-termination complexes (harboring peptidyl-tRNA) are not recycled by RRF and EFG in vitro, suggesting participation of additional factor(s) in the process. Using a combination of biochemical and genetic approaches, we show that, (i) Inclusion of IF3 with RRF and EFG results in recycling of the pre-termination complexes; (ii) IF3 overexpression in Escherichia coli LJ14 rescues its temperature sensitive phenotype for RRF; (iii) Transduction of infC135 (which encodes a functionally compromised IF3) in E.coli LJ14 generates a ‘synthetic severe’ phenotype; (iv) The infC135 and frr1 (containing an insertion in the RRF gene promoter) alleles synergistically rescue a temperature sensitive mutation in peptidyl-tRNA hydrolase in E.coli; and (v) IF3 facilitates ribosome recycling by Thermus thermophilus RRF and E.coli EFG in vivo and in vitro. These lines of evidence clearly demonstrate the physiological importance of IF3 in the overall mechanism of ribosome recycling in E.coli.


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