| RRC ID |
66203
|
| 著者 |
Wamp S, Rutter ZJ, Rismondo J, Jennings CE, Möller L, Lewis RJ, Halbedel S.
|
| タイトル |
PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM.
|
| ジャーナル |
Elife
|
| Abstract |
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.
|
| 巻・号 |
9
|
| 公開日 |
2020-5-29
|
| DOI |
10.7554/eLife.56048
|
| PII |
56048
|
| PMID |
32469310
|
| PMC |
PMC7286690
|
| MeSH |
Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Listeria monocytogenes / genetics
Listeria monocytogenes / metabolism
Muramidase / genetics
Muramidase / metabolism
Peptidoglycan / biosynthesis*
Peptidoglycan / genetics
Peptidoglycan / metabolism
Phosphorylation
Protein Serine-Threonine Kinases / genetics
Protein Serine-Threonine Kinases / metabolism*
Suppression, Genetic / genetics
|
| IF |
7.08
|
| リソース情報 |
| 原核生物(大腸菌) |
|
