NDLI: Regulation of Expression of the vanD Glycopeptide Resistance Gene Cluster from Enterococcus faecium BM4339

Content Provider	PubMed Central
Author	Barbara, Casadewall Reynolds, Peter E. Patrice, Courvalin
Copyright Year	2001
Abstract	A new open reading frame, encoding a putative integrase-like protein, was detected downstream from the six genes of the vanD glycopeptide resistance cluster in Enterococcus faecium BM4339 (B. Casadewall and P. Courvalin, J. Bacteriol. 181:3644–3648, 1999). In this cluster, genes coding for the VanRD-VanSD two-component regulatory system were cotranscribed from the P RD promoter, whereas transcription of the vanYD, vanHD, vanD, vanXD , and intD genes was initiated from the P YD promoter located between vanSD and vanYD (the D subscript indicates that the gene is part of the vanD operon). The VanRD-VanSD regulatory system is likely to activate transcription of the resistance genes from the promoter P YD . Glycopeptide-susceptible derivatives of BM4339 were obtained by trans complementation of the frameshift mutation in the ddl gene, restoring functional d-alanine:d-alanine ligase activity in this strain. The glycopeptide-susceptible transformant BM4409, producing only d-alanyl-d-alanine-terminating peptidoglycan precursors, did not express the resistance genes encoding the VanYD d,d-carboxypeptidase, the VanHD dehydrogenase, the VanD ligase, the VanXD d,d-dipeptidase, and also the IntD integrase, although the regulatory region of the vanD cluster was still transcribed. In BM4409, the absence of VanRD-VanSD, apparently dependent, transcription from promoter P YD correlated with the lack of d-alanyl-d-lactate-terminating precursors. The vanXD gene was transcribed in BM4339, but detectable amounts of VanXD d,d-dipeptidase were not synthesized. However, the gene directed synthesis of an active enzyme when cloned on a multicopy plasmid in Escherichia coli, suggesting that the enzyme was unstable in BM4339 or that it had very low activity that was detectable only under conditions of high gene dosage. This activity is not required for glycopeptide resistance in BM4339, since this strain cannot synthesize d-alanyl-d-alanine.
Related Links	http://dx.doi.org/10.1128/jb.183.11.3436-3446.2001
Ending Page	3446
Page Count	11
Starting Page	3436
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	11
Volume Number	183
Language	English
Publisher	American Society for Microbiology
Publisher Date	2001-06-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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