IMR Press / FBL / Volume 4 / Issue 4 / DOI: 10.2741/macinga

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


The chromosomal 2'-N-acetyltransferase of Providencia stuartii: physiological functions and genetic regulation

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1 Division of Infectious Diseases, Case Western Reserve University, 10900 Euclid Ave, Cleveland, OH 44106, USA
2 Departments of Medicine and of Molecular Biology and Microbiology, Case Western Reserve University, 10900 Euclid Ave, Cleveland, OH 44106, USA
Front. Biosci. (Landmark Ed) 1999, 4(4), 132–140;
Published: 1 February 1999

Intrinsic chromosomal acetyltransferases involved in aminoglycoside resistance have been identified in a number of bacteria. In Providencia stuartii, a chromosomal acetyltransferase (AAC(2')-Ia) has been characterized in detail. In addition to the ability to acetylate aminoglycosides, the AAC(2')-Ia enzyme has at least one physiological function, which is the acetylation of peptidoglycan. This modification is likely to influence the autolytic system in P. stuartii. The regulation of aac(2')-Ia expression is extremely complex involving at least seven regulatory genes acting in at least two pathways. This complexity in regulation indicates that aac(2')-Ia expression must be tightly controlled in response to different environmental conditions. This presumably reflects the importance of maintaining correct levels of peptidoglycan acetylation. In this review, a summary of data will be presented involving both the physiological and genetic aspects of aac(2')-Ia in P. stuartii.

Aminoglycoside Resistance
Gene Regulation
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