Regulated Cleavage of Glycan Strands by the Murein Hydrolase SagB in Staphylococcus aureus Involves a Direct Interaction with LyrA (SpdC)
Stephanie E. Willing, Olaf Schneewind, Dominique Missiakas
Abstract
is associated with longer glycan strands in peptidoglycan, altered protein trafficking and secretion in the envelope, and aberrant excretion of cytosolic proteins. It is not clear whether SagB, with its single transmembrane segment, serves as the molecular ruler of glycan chains or whether other factors modulate its activity. Here, we show that LyrA (SpdC), a protein of the CAAX type II prenyl endopeptidase family, modulates SagB activity via interaction though its transmembrane domain.
Topics & Concepts
PeptidoglycanGlycanBiologyLipid IIStaphylococcus aureusCleavage (geology)BiochemistryCell biologyMembraneHydrolaseGlycoside hydrolaseCell membraneBiophysicsMicrobiologyCell wallEnzymeBacteriaGlycoproteinGeneticsFracture (geology)PaleontologyBiochemical and Structural CharacterizationAntimicrobial Resistance in StaphylococcusCarbohydrate Chemistry and Synthesis