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PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM
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PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM
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Journal Article
PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM
2020
Overview
Peptidoglycan (PG) is the main component of bacterial cell walls and the target for many antibiotics. PG biosynthesis is tightly coordinated with cell wall growth and turnover, and many of these control activities depend upon PASTA-domain containing eukaryotic-like serine/threonine protein kinases (PASTA-eSTK) that sense PG fragments. However, only a few PG biosynthetic enzymes are direct kinase substrates. Here, we identify the conserved ReoM protein as a novel PASTA-eSTK substrate in the Gram-positive pathogen Listeria monocytogenes. Our data show that the phosphorylation of ReoM is essential as it controls ClpCP-dependent proteolytic degradation of the essential enzyme MurA, which catalyses the first committed step in PG biosynthesis. We also identify ReoY as a second novel factor required for degradation of ClpCP substrates. Collectively, our data imply that the first committed step of PG biosynthesis is activated through control of ClpCP protease activity in response to signals of PG homeostasis imbalance.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ Bacteria
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Enzymes
/ Genes
/ Kinases
/ Lipids
/ Listeria
/ Listeria monocytogenes - genetics
/ Listeria monocytogenes - metabolism
/ Microbiology and Infectious Disease
/ Mutation
/ Novels
/ Peptidoglycan - biosynthesis
/ Protein-Serine-Threonine Kinases - genetics
/ Protein-Serine-Threonine Kinases - metabolism
/ Proteins
/ Serine
/ serine/threonine protein kinase
