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Journal of Bacteriology, September 2008, p. 5862-5869, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00632-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Effects on Translation Pausing of Alterations in Protein and RNA Components of the Ribosome Exit Tunnel{triangledown}

Marlon G. Lawrence, Lasse Lindahl, and Janice M. Zengel*

Department of Biological Sciences, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, Maryland 21250

Received 6 May 2008/ Accepted 22 June 2008

Amino acids are polymerized into peptides in the peptidyl transferase center of the ribosome. The nascent peptides then pass through the exit tunnel before they reach the extraribosomal environment. A number of nascent peptides interact with the exit tunnel and stall elongation at specific sites within their peptide chain. Several mutational changes in RNA and protein components of the ribosome have previously been shown to interfere with pausing. These changes are localized in the narrowest region of the tunnel, near a constriction formed by ribosomal proteins L4 and L22. To expand our knowledge about peptide-induced pausing, we performed a comparative study of pausing induced by two peptides, SecM and a short peptide, CrbCmlA, that requires chloramphenicol as a coinducer of pausing. We analyzed the effects of 15 mutational changes in L4 and L22, as well as the effects of methylating nucleotide A2058 of 23S rRNA, a nucleotide previously implicated in pausing and located close to the L4-L22 constriction. Our results show that methylation of A2058 and most mutational changes in L4 and L22 have differential effects on pausing in response to CrbCmlA and SecM. Only one change, a 6-amino-acid insertion after amino acid 72 in L4, affects pausing in both peptides. We conclude that the two peptides interact with different regions of the exit tunnel. Our results suggest that either the two peptides use different mechanisms of pausing or they interact differently but induce similar inhibitory conformational changes in functionally important regions of the ribosome.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250. Phone: (410) 455-2876. Fax: (410) 455-3875. E-mail: zengel{at}umbc.edu

{triangledown} Published ahead of print on 27 June 2008.

Journal of Bacteriology, September 2008, p. 5862-5869, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00632-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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