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SirA inhibits the essential DnaA:DnaD interaction to block helicase recruitment during Bacillus subtilis sporulation.

Winterhalter, C ; Stevens, D ; et al.
In: Nucleic acids research, Jg. 51 (2023-05-22), Heft 9, S. 4302-4321
academicJournal

Bidirectional DNA replication from a chromosome origin requires the asymmetric loading of two helicases, one for each replisome. Our understanding of the molecular mechanisms underpinning helicase loading at bacterial chromosome origins is incomplete. Here we report both positive and negative mechanisms for directing helicase recruitment in the model organism Bacillus subtilis. Systematic characterization of the essential initiation protein DnaD revealed distinct protein interfaces required for homo-oligomerization, interaction with the master initiator protein DnaA, and interaction with the helicase co-loader protein DnaB. Informed by these properties of DnaD, we went on to find that the developmentally expressed repressor of DNA replication initiation, SirA, blocks the interaction between DnaD and DnaA, thereby restricting helicase recruitment from the origin during sporulation to inhibit further initiation events. These results advance our understanding of the mechanisms underpinning DNA replication initiation in B. subtilis, as well as guiding the search for essential cellular activities to target for antimicrobial drug design.

(© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.)

Titel:
SirA inhibits the essential DnaA:DnaD interaction to block helicase recruitment during Bacillus subtilis sporulation.
Autor/in / Beteiligte Person: Winterhalter, C ; Stevens, D ; Fenyk, S ; Pelliciari, S ; Marchand, E ; Soultanas, P ; Ilangovan, A ; Murray, H
Zeitschrift: Nucleic acids research, Jg. 51 (2023-05-22), Heft 9, S. 4302-4321
Veröffentlichung: 1992- : Oxford : Oxford University Press ; <i>Original Publication</i>: London, Information Retrieval ltd., 2023
Medientyp: academicJournal
ISSN: 1362-4962 (electronic)
DOI: 10.1093/nar/gkac1060
Schlagwort:
  • DNA Replication
  • DNA-Binding Proteins genetics
  • DNA-Binding Proteins metabolism
  • DnaB Helicases genetics
  • DnaB Helicases metabolism
  • Replication Origin
  • Bacillus subtilis genetics
  • Bacillus subtilis metabolism
  • Bacillus subtilis physiology
  • Bacterial Proteins genetics
  • Bacterial Proteins metabolism
  • DNA Helicases genetics
  • DNA Helicases metabolism
  • Spores, Bacterial metabolism
Sonstiges:
  • Nachgewiesen in: MEDLINE
  • Sprachen: English
  • Publication Type: Journal Article; Research Support, Non-U.S. Gov't
  • Language: English
  • [Nucleic Acids Res] 2023 May 22; Vol. 51 (9), pp. 4302-4321.
  • MeSH Terms: Bacillus subtilis* / genetics ; Bacillus subtilis* / metabolism ; Bacillus subtilis* / physiology ; Bacterial Proteins* / genetics ; Bacterial Proteins* / metabolism ; DNA Helicases* / genetics ; DNA Helicases* / metabolism ; Spores, Bacterial* / metabolism ; DNA Replication ; DNA-Binding Proteins / genetics ; DNA-Binding Proteins / metabolism ; DnaB Helicases / genetics ; DnaB Helicases / metabolism ; Replication Origin
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  • Grant Information: United Kingdom WT_ Wellcome Trust; 204985/Z/16/Z United Kingdom WT_ Wellcome Trust; BB/P018432/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council
  • Substance Nomenclature: 0 (Bacterial Proteins) ; EC 3.6.4.- (DNA Helicases) ; 0 (DNA-Binding Proteins) ; EC 3.6.4.12 (DnaB Helicases)
  • Entry Date(s): Date Created: 20221123 Date Completed: 20230524 Latest Revision: 20230524
  • Update Code: 20231215
  • PubMed Central ID: PMC10201431

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