Roles of RodZ and class A PBP1b in the assembly and regulation of the peripheral peptidoglycan elongasome in ovoid-shaped cells of Streptococcus pneumoniae D39.

class A PBP function and regulation elongasome assembly peptidoglycan synthesis synthetic-viable genetic relationships

Journal

Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028

Informations de publication

Date de publication:
10 2022
Historique:
revised: 30 07 2022
received: 02 06 2022
accepted: 02 08 2022
pubmed: 25 8 2022
medline: 26 10 2022
entrez: 24 8 2022
Statut: ppublish

Résumé

RodZ of rod-shaped bacteria functions to link MreB filaments to the Rod peptidoglycan (PG) synthase complex that moves circumferentially perpendicular to the long cell axis, creating hoop-like sidewall PG. Ovoid-shaped bacteria, such as Streptococcus pneumoniae (pneumococcus; Spn) that lack MreB, use a different modality for peripheral PG elongation that emanates from the midcell of dividing cells. Yet, S. pneumoniae encodes a RodZ homolog similar to RodZ in rod-shaped bacteria. We show here that the helix-turn-helix and transmembrane domains of RodZ(Spn) are essential for growth at 37°C. ΔrodZ mutations are suppressed by Δpbp1a, mpgA(Y488D), and ΔkhpA mutations that suppress ΔmreC, but not ΔcozE. Consistent with a role in PG elongation, RodZ(Spn) co-localizes with MreC and aPBP1a throughout the cell cycle and forms complexes and interacts with PG elongasome proteins and regulators. Depletion of RodZ(Spn) results in aberrantly shaped, non-growing cells and mislocalization of elongasome proteins MreC, PBP2b, and RodA. Moreover, Tn-seq reveals that RodZ(Spn), but not MreCD(Spn), displays a specific synthetic-viable genetic relationship with aPBP1b, whose function is unknown. We conclude that RodZ(Spn) acts as a scaffolding protein required for elongasome assembly and function and that aPBP1b, like aPBP1a, plays a role in elongasome regulation and possibly peripheral PG synthesis.

Identifiants

pubmed: 36001060
doi: 10.1111/mmi.14969
pmc: PMC9804626
doi:

Substances chimiques

Peptidoglycan 0
Bacterial Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

336-368

Subventions

Organisme : NIAID NIH HHS
ID : F31 AI138430
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM141242
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131767
Pays : United States
Organisme : NIH HHS
ID : S10 OD024988
Pays : United States

Informations de copyright

© 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.

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Auteurs

Melissa M Lamanna (MM)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Irfan Manzoor (I)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Merrin Joseph (M)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Ziyun A Ye (ZA)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Mattia Benedet (M)

Department of Cellular, Computational and Integrative Biology (CIBIO), University of Trento, Trento, Italy.

Alessia Zanardi (A)

Department of Cellular, Computational and Integrative Biology (CIBIO), University of Trento, Trento, Italy.

Zhongqing Ren (Z)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Xindan Wang (X)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Orietta Massidda (O)

Department of Cellular, Computational and Integrative Biology (CIBIO), University of Trento, Trento, Italy.

Ho-Ching T Tsui (HT)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

Malcolm E Winkler (ME)

Department of Biology, Indiana University Bloomington, Bloomington, Indiana, USA.

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