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The glucosaminidase domain of Atl - the major Staphylococcus aureus autolysin - has DNA-binding activity.

ABSTRACT: In this communication, we describe evidence demonstrating the capacity of Atl, the major Staphylococcus aureus autolytic enzyme to bind DNA. Electrophoretic mobility shift assays (EMSA) show that both the Atl protein and the endo-?-N-acetylglucosaminidase (GL) domain were able to bind DNA of nonspecific sequence. The implications of this unexpected observation for the physiology of S. aureus remain to be explored.

SUBMITTER: Grilo IR

PROVIDER: S-EPMC3996572 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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The glucosaminidase domain of Atl - the major Staphylococcus aureus autolysin - has DNA-binding activity.

Grilo Inês R IR Ludovice Ana Madalena AM Tomasz Alexander A de Lencastre Hermínia H Sobral Rita G RG

MicrobiologyOpen 20140303 2

In this communication, we describe evidence demonstrating the capacity of Atl, the major Staphylococcus aureus autolytic enzyme to bind DNA. Electrophoretic mobility shift assays (EMSA) show that both the Atl protein and the endo-β-N-acetylglucosaminidase (GL) domain were able to bind DNA of nonspecific sequence. The implications of this unexpected observation for the physiology of S. aureus remain to be explored. ...[more]

PMID: 24585695

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Project description:The peptidoglycan of the bacterial cell wall undergoes a permanent turnover during cell growth and differentiation. In the Gram-positive pathogen Staphylococcus aureus, the major peptidoglycan hydrolase Atl is required for accurate cell division, daughter cell separation and autolysis. Atl is a bifunctional N-acetylmuramoyl-L-alanine amidase/endo-?-N-acetylglucosaminidase that releases peptides and the disaccharide N-acetylmuramic acid-?-1,4-N-acetylglucosamine (MurNAc-GlcNAc) from the peptido-glycan. Here we revealed the recycling pathway of the cell wall turnover product MurNAc-GlcNAc in S. aureus. The latter disaccharide is internalized and concomitantly phosphorylated by the phosphotransferase system (PTS) transporter MurP, which had been implicated previously in the uptake and phosphorylation of MurNAc. Since MurP mutant cells accumulate MurNAc-GlcNAc and not MurNAc in the culture medium during growth, the disaccharide represents the physiological substrate of the PTS transporter. We further identified and characterized a novel 6-phospho-N-acetylmuramidase, named MupG, which intracellularly hydrolyses MurNAc 6-phosphate-GlcNAc, the product of MurP-uptake and phosphorylation, yielding MurNAc 6-phosphate and GlcNAc. MupG is the first characterized representative of a novel family of glycosidases containing domain of unknown function 871 (DUF871). The corresponding gene mupG (SAUSA300_0192) of S. aureus strain USA300 is the first gene within a putative operon that also includes genes encoding the MurNAc 6-phosphate etherase MurQ, MurP, and the putative transcriptional regulator MurR. Using mass spectrometry, we observed cytoplasmic accumulation of MurNAc 6-phosphate-GlcNAc in ?mupG and ?mupGmurQ markerless non-polar deletion mutants, but not in the wild type or in the complemented ?mupG strain. MurNAc 6-phosphate-GlcNAc levels in the mutants increased during stationary phase, in accordance with previous observations regarding peptidoglycan recycling in S. aureus.

Dataset Information

The glucosaminidase domain of Atl - the major Staphylococcus aureus autolysin - has DNA-binding activity.

Publications

The glucosaminidase domain of Atl - the major Staphylococcus aureus autolysin - has DNA-binding activity.

Similar Datasets

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