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Journal of Bacteriology, April 2009, p. 2894-2898, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01715-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

ClpXP Degrades SsrA-Tagged Proteins in Streptococcus pneumoniae{triangledown}

Sarita Ahlawat and Donald A. Morrison*

Laboratory for Molecular Biology, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607

Received 8 December 2008/ Accepted 5 February 2009

Bacterial proteins that are abnormally truncated due to incomplete mRNA or the presence of rare codons are extended by an SsrA tag during ribosome rescue in a trans-translation process important for maintaining protein quality. In Escherichia coli, the SsrA-tagged proteins become the target of the Tsp, Lon, FtsH, ClpXP, and ClpAP proteases. Here we show that degradation of model SsrA-tagged proteins in Streptococcus pneumoniae depends primarily or exclusively on ClpXP in vivo. In addition, we show the E. coli SsrA tag is also a target of S. pneumoniae ClpXP in vivo, even though the N-terminal portions of the tags differ significantly between the two species, suggesting there may be no adaptor protein for SsrA in S. pneumoniae.

* Corresponding author. Mailing address: LMB Room 4150, 900 South Ashland Ave., Chicago, IL 60607. Phone: (312) 996-6839. Fax: (312) 413-2691. E-mail: DAMorris{at}uic.edu

{triangledown} Published ahead of print on 13 February 2009.

Journal of Bacteriology, April 2009, p. 2894-2898, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01715-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Piotrowski, A., Burghout, P., Morrison, D. A. (2009). spr1630 Is Responsible for the Lethality of clpX Mutations in Streptococcus pneumoniae. J. Bacteriol. 191: 4888-4895 [Abstract] [Full Text]  


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