PMID:10464220
| Citation |
Stohl, EA, Brady, SF, Clardy, J and Handelsman, J (1999) ZmaR, a novel and widespread antibiotic resistance determinant that acetylates zwittermicin A. J. Bacteriol. 181:5455-60 |
|---|---|
| Abstract |
ZmaR is a resistance determinant of unusual abundance in the environment and confers on gram-positive and gram-negative bacteria resistance to zwittermicin A, a novel broad-spectrum antibiotic produced by species of Bacillus. The ZmaR protein has no sequence similarity to proteins of known function; thus, the purpose of the present study was to determine the function of ZmaR in vitro. Cell extracts of E. coli containing zmaR inactivated zwittermicin A by covalent modification. Chemical analysis of inactivated zwittermicin A by 1H NMR, 13C NMR, and high- and low-resolution mass spectrometry demonstrated that the inactivated zwittermicin A was acetylated. Purified ZmaR protein inactivated zwittermicin A, and biochemical assays for acetyltransferase activity with [14C]acetyl coenzyme A demonstrated that ZmaR catalyzes the acetylation of zwittermicin A with acetyl coenzyme A as a donor group, suggesting that ZmaR may constitute a new class of acetyltransferases. Our results allow us to assign a biochemical function to a resistance protein that has no sequence similarity to proteins of known function, contributing fundamental knowledge to the fields of antibiotic resistance and protein function. |
| Links | |
| Keywords |
Acetylation; Acetyltransferases/metabolism; Anti-Bacterial Agents/chemistry; Anti-Bacterial Agents/metabolism; Bacterial Proteins/metabolism; Drug Resistance, Microbial; Molecular Structure; Peptides |
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