Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall. Academic Article

abstract

• Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion. However, the mechanisms of their coordination remain elusive. Moenomycin that inhibits a family of PG synthases known as Class-A penicillin-binding proteins (aPBPs), collapses rod shape despite aPBPs being non-essential for rod-like morphology in the bacterium Myxococcus xanthus. Here, we demonstrate that inhibited PBP1a2, an aPBP, accelerates the degradation of cell poles by DacB, a hydrolytic PG peptidase. Moenomycin promotes the binding between DacB and PG and thus reduces the mobility of DacB through PBP1a2. Conversely, DacB also regulates the distribution and dynamics of aPBPs. Our findings clarify the action of moenomycin and suggest that disrupting the coordination between PG synthases and hydrolases could be more lethal than eliminating individual enzymes.

authors

• Nan, Beiyan

published proceedings

• Nat Commun

author list (cited authors)

• Zhang, H., Venkatesan, S., Ng, E., & Nan, B.

complete list of authors

• Zhang, Huan||Venkatesan, Srutha||Ng, Emily||Nan, Beiyan

publication date

• September 2023

publisher

• Springer Nature  Publisher

published in

• Nature Communications  Journal

keywords

• Bambermycins
• Cell Wall
• Myxococcus Xanthus
• Nitric Oxide Synthase
• Penicillin-binding Proteins
• Peptide Hydrolases
• Peptidoglycan

PubMed Central ID

• 37660104

Digital Object Identifier (DOI)

• 10.1038/s41467-023-41082-3

start page

• 5357

volume

• 14

issue

• 1

URL

• http://dx.doi.org/10.1038/s41467-023-41082-3