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Alterations in the two globular domains or in the connecting alpha-helix of bacterial ribosomal protein L9 induces +1 frameshifts.
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). (Björk)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). (Björk)
2007 (English)In: J Bacteriol, ISSN 0021-9193, Vol. 189, no 19, 7024-31 p.Article in journal (Refereed) Published
Abstract [en]

The ribosomal 50S subunit protein L9, encoded by the gene rplI, is an elongated protein with an alpha-helix connecting the N- and C-terminal globular domains. We isolated rplI mutants that suppress the +1 frameshift mutation hisC3072 in Salmonella enterica serovar Typhimurium. These mutants have amino acid substitutions in the N-terminal domain (G24D) or in the C-terminal domain (I94S, A102D, G126V, and F132S) of L9. In addition, different one-base deletions in rplI altered either the final portion of the C terminus or removed the C-terminal domain with or without the connecting alpha-helix. An alanine-to-proline substitution at position 59 (A59P), which breaks the alpha-helix between the globular domains, induced +1 frameshifting, suggesting that the geometrical relationship between the N and C domains is important to maintain the reading frame. Except for the alterations G126V in the C terminus and A59P in the connecting alpha-helix, our results confirm earlier results obtained by using the phage T4 gene 60-based system to monitor bypassing. The way rplI mutations suppress various frameshift mutations suggests that bypassing of many codons from several takeoff and landing sites occurred instead of a specific frameshift forward at overlapping codons.

Place, publisher, year, edition, pages
2007. Vol. 189, no 19, 7024-31 p.
Identifiers
URN: urn:nbn:se:umu:diva-16716PubMedID: 17660285OAI: oai:DiVA.org:umu-16716DiVA: diva2:156389
Available from: 2007-10-09 Created: 2007-10-09 Last updated: 2010-04-22Bibliographically approved

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Björk, Glenn R

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CiteExportLink to record
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