Distinct Amino Acid Availability-Dependent Regulatory Mechanisms of MepS and MepM Levels in Escherichia coli
Autor: | Han Byeol Lee, Byoung Jun Choi, Umji Choi, Ji Eun Son, Si Hyoung Park, Yung Jae Kim, Chang-Ro Lee, Won-Jae Chi |
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Rok vydání: | 2021 |
Předmět: |
Microbiology (medical)
peptidoglycan hydrolase peptidoglycan endopeptidase Proteolysis medicine.medical_treatment Mutant medicine.disease_cause Microbiology amino acid availability 03 medical and health sciences chemistry.chemical_compound MepS Aromatic amino acids medicine Escherichia coli Original Research 030304 developmental biology chemistry.chemical_classification 0303 health sciences Protease medicine.diagnostic_test 030306 microbiology MepM Periplasmic space QR1-502 Amino acid chemistry Biochemistry NlpI Peptidoglycan Prc |
Zdroj: | Frontiers in Microbiology Frontiers in Microbiology, Vol 12 (2021) |
ISSN: | 1664-302X |
DOI: | 10.3389/fmicb.2021.677739 |
Popis: | Peptidoglycan (PG) hydrolases play important roles in various aspects of bacterial physiology, including cytokinesis, PG synthesis, quality control of PG, PG recycling, and antibiotic resistance. However, the regulatory mechanisms of their expression are poorly understood. In this study, we have uncovered novel regulatory mechanisms of the protein levels of the synthetically lethal PG endopeptidases MepS and MepM, which are involved in PG synthesis. A mutant defective for both MepS and MepM was lethal in an amino acid-rich medium, whereas it exhibited almost normal growth in a minimal medium, suggesting the expendability of MepS and MepM in a minimal medium. Protein levels of MepS and MepM dramatically decreased in the minimal medium. Although MepM was revealed as a substrate of Prc, a periplasmic protease involved in the proteolysis of MepS, only the decrease in the MepS level in the minimal medium was affected by theprcdepletion. Phenotypic and biochemical analyses showed that the presence of aromatic amino acids in the medium induced the accumulation of MepS, but not MepM, while the presence of glutamate increased the level of MepM, but not MepS. Together, these results demonstrate that the protein levels of the two major PG endopeptidases are regulated in an amino acid availability-dependent manner, but their molecular mechanisms and signaling are significantly distinct. |
Databáze: | OpenAIRE |
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