Functional redundancy between penicillin-binding proteins during asymmetric cell division in <i>Clostridioides difficile</i>.

ABSTRACT: Peptidoglycan synthesis is an essential driver of bacterial growth and division. The final steps of this crucial process involve the activity of the SEDS family glycosyltransferases that polymerize glycan strands and the class B penicillin-binding protein (bPBP) transpeptidases that cross-link them. While many bacteria encode multiple bPBPs to perform specialized roles during specific cellular processes, some bPBPs can play redundant roles that are important for resistance against certain cell wall stresses. Our understanding of these compensatory mechanisms, however, remains incomplete. Endospore-forming bacteria typically encode multiple bPBPs that drive morphological changes required for sporulation. The sporulation-specific bPBP, SpoVD, is important for synthesizing the asymmetric divi

SUBMITTER: Shrestha S 

PROVIDER: S-EPMC11463367 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature