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Unipolar Peptidoglycan Synthesis in the Rhizobiales Requires an Essential Class A Penicillin-Binding Protein
Division of Biological Sciences, University of Missouri, Columbia, Missouri, USA.
Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
Center for Synthetic Microbiology (SYNMIKRO), Philipps University Marburg, Marburg, Germany; Department of Biology, Philipps University Marburg, Marburg, Germany.
Department of Chemistry, Indiana University, IN, Bloomington, United States.
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2021 (Engelska)Ingår i: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 12, nr 5, artikel-id e0234621Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Members of the Rhizobiales are polarly growing bacteria that lack homologs of the canonical Rod complex. To investigate the mechanisms underlying polar cell wall synthesis, we systematically probed the function of cell wall synthesis enzymes in the plant pathogen Agrobacterium tumefaciens. The development of fluorescent d-amino acid dipeptide (FDAAD) probes, which are incorporated into peptidoglycan by penicillin-binding proteins in A. tumefaciens, enabled us to monitor changes in growth patterns in the mutants. Use of these fluorescent cell wall probes and peptidoglycan compositional analysis demonstrate that a single class A penicillin-binding protein is essential for polar peptidoglycan synthesis. Furthermore, we find evidence of an additional mode of cell wall synthesis that requires ld-transpeptidase activity. Genetic analysis and cell wall targeting antibiotics reveal that the mechanism of unipolar growth is conserved in Sinorhizobium and Brucella. This work provides insights into unipolar peptidoglycan biosynthesis employed by the Rhizobiales during cell elongation.

IMPORTANCE

While the structure and function of the bacterial cell wall are well conserved, the mechanisms responsible for cell wall biosynthesis during elongation are variable. It is increasingly clear that rod-shaped bacteria use a diverse array of growth strategies with distinct spatial zones of cell wall biosynthesis, including lateral elongation, unipolar growth, bipolar elongation, and medial elongation. Yet the vast majority of our understanding regarding bacterial elongation is derived from model organisms exhibiting lateral elongation. Here, we explore the role of penicillin-binding proteins in unipolar elongation of Agrobacterium tumefaciens and related bacteria within the Rhizobiales. Our findings suggest that penicillin-binding protein 1a, along with a subset of ld-transpeptidases, drives unipolar growth. Thus, these enzymes may serve as attractive targets for biocontrol of pathogenic Rhizobiales.

Ort, förlag, år, upplaga, sidor
ASM International, 2021. Vol. 12, nr 5, artikel-id e0234621
Nyckelord [en]
Agrobacterium tumefaciens, cell envelope, cell wall, penicillin-binding proteins, peptidoglycan, polar growth, Rhizobiales
Nationell ämneskategori
Mikrobiologi inom det medicinska området Mikrobiologi
Forskningsämne
mikrobiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-190608DOI: 10.1128/mBio.02346-21ISI: 000744191100005PubMedID: 34544272Scopus ID: 2-s2.0-85121014637OAI: oai:DiVA.org:umu-190608DiVA, id: diva2:1621759
Tillgänglig från: 2021-12-20 Skapad: 2021-12-20 Senast uppdaterad: 2023-09-05Bibliografiskt granskad

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Aliashkevich, Alena

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Aliashkevich, AlenaCava, Felipe
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Molekylär Infektionsmedicin, Sverige (MIMS)Umeå Centre for Microbial Research (UCMR)Institutionen för molekylärbiologi (Medicinska fakulteten)
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