Localization characteristics of cell wall synthesis protein Wag31 and penicillin binding protein C in <i>Clavibacter michiganensis</i>.

ABSTRACT: CmWag31 is a member of the DivIVA family of proteins in Clavibacter michiganensis. The DivIVA family have been demonstrated to play a key role in the synthesis of cell wall peptidoglycan and cell division in most bacterial species. It has been previously confirmed that the pbpC (penicillin-binding protein C) deletion mutants affect bacterial division and cell wall synthesis. Based on the confirmation of the interaction between CmWag31 and CmPBPC, the present study conducted a systemic analysis on their localization characteristics. The results indicated that CmWag31 exhibited the capacity to interact with the transglycosylase (TG) and transpeptidase (TP) domain of CmPBPC, while CmPBPC only interacted with the NTD region of CmWag31. Co-localization analysis showed that CmWag31

SUBMITTER: Yu C 

PROVIDER: S-EPMC12445707 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature