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Journal of Bacteriology, August 2009, p. 4888-4895, Vol. 191, No. 15
0021-9193/09/$08.00+0     doi:10.1128/JB.00285-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

spr1630 Is Responsible for the Lethality of clpX Mutations in Streptococcus pneumoniae{triangledown}

Andrew Piotrowski,1 Peter Burghout,2 and Donald A. Morrison1*

Laboratory for Molecular Biology, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Ilinois 60607,1 Laboratory of Pediatric Infectious Diseases, Nijmegen Medical Centre, 6500 HB Nijmegen, The Netherlands2

Received 3 March 2009/ Accepted 12 May 2009

The Clp protease ATPase subunit and chaperone ClpX is dispensable in some bacteria, but it is thought to be essential in others, including streptococci and lactococci. We confirm that clpX is essential in the Rx strain of Streptococcus pneumoniae but show that the requirement for clpX can be relieved by point mutations, frame shifts, or deletion of the gene spr1630, which is found in many isolates of S. pneumoniae. Homologs occur frequently in Staphylococcus aureus as well as in a few strains of Listeria monocytogenes, Lactobacillus johnsonii, and Lactobacillus rhamnosus. In each case, the spr1630 homolog is accompanied by a putative transcriptional regulator with an HTH DNA binding motif. In S. pneumoniae, the spr1630-spr1629 gene pair, accompanied by a RUP element, occurs as an island inserted between the trpA and cclA genes in 15 of 22 sequenced genomes.

* 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 22 May 2009.

Journal of Bacteriology, August 2009, p. 4888-4895, Vol. 191, No. 15
0021-9193/09/$08.00+0     doi:10.1128/JB.00285-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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