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Journal of Bacteriology, April 2009, p. 2721-2727, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.00024-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

LpqM, a Mycobacterial Lipoprotein-Metalloproteinase, Is Required for Conjugal DNA Transfer in Mycobacterium smegmatis{triangledown}

Kiet T. Nguyen,1,§ Kristina Piastro,1,{dagger} and Keith M. Derbyshire1,2*

Division of Genetics, Wadsworth Center, New York State Department of Health,1 Department of Biomedical Sciences, School of Public Health, University at Albany, Albany, New York 122012

Received 9 January 2009/ Accepted 10 February 2009

We have previously described a novel conjugal DNA transfer process that occurs in Mycobacterium smegmatis. To identify donor genes required for transfer, we have performed a transposon mutagenesis screen; we report here that LpqM, a putative lipoprotein-metalloproteinase, is essential for efficient DNA transfer. Bioinformatic analyses predict that LpqM contains a signal peptide necessary for the protein's targeting to the cell envelope and a metal ion binding motif, the likely catalytic site for protease activity. Using targeted mutagenesis, we demonstrate that each of these motifs is necessary for DNA transfer and that LpqM is located in the cell envelope. The requirement for transfer is specific to the donor strain; an lpqM knockout mutant in the recipient is still proficient in transfer assays. The activity of LpqM is conserved among mycobacteria; homologues from both Mycobacterium tuberculosis and Mycobacterium avium can complement lpqM donor mutants, suggesting that the homologues recognize and process similar proteins. Lipoproteins constitute a significant proportion of the mycobacterial cell wall, but despite their abundance, very few have been assigned an activity. We discuss the potential role of LpqM in DNA transfer and the implications of the conservation of LpqM activity in M. tuberculosis.

* Corresponding author. Mailing address: Wadsworth Center, NYS Department of Health, P.O. Box 509, Albany, NY 12201. Phone: (518) 473-6079. Fax: (518) 474-3181. E-mail: keith.derbyshire{at}wadsworth.org

{triangledown} Published ahead of print on 20 February 2009.

§ Present address: National Center for Toxicological Research, 3900 NCTR, Jefferson, AR 72079.

{dagger} Present address: University at Buffalo School of Medicine and Biomedical Sciences, 155 Biomedical Education Building, Buffalo, NY 14214.

Journal of Bacteriology, April 2009, p. 2721-2727, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.00024-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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