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TitleStaphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.
Journal, issue, pagesNucleic Acids Res, Vol. 50, Issue 14, Page 8349-8362, Year 2022
Publish dateAug 12, 2022
AuthorsCuncun Qiao / Gianluca Debiasi-Anders / Ignacio Mir-Sanchis /
PubMed AbstractReplication is a crucial cellular process. Replicative helicases unwind DNA providing the template strand to the polymerase and promoting replication fork progression. Helicases are multi-domain ...Replication is a crucial cellular process. Replicative helicases unwind DNA providing the template strand to the polymerase and promoting replication fork progression. Helicases are multi-domain proteins which use an ATPase domain to couple ATP hydrolysis with translocation, however the role that the other domains might have during translocation remains elusive. Here, we studied the unexplored self-loading helicases called Reps, present in Staphylococcus aureus pathogenicity islands (SaPIs). Our cryoEM structures of the PriRep5 from SaPI5 (3.3 Å), the Rep1 from SaPI1 (3.9 Å) and Rep1-DNA complex (3.1Å) showed that in both Reps, the C-terminal domain (CTD) undergoes two distinct movements respect the ATPase domain. We experimentally demonstrate both in vitro and in vivo that SaPI-encoded Reps need key amino acids involved in the staircase mechanism of translocation. Additionally, we demonstrate that the CTD's presence is necessary for the maintenance of full ATPase and helicase activities. We speculate that this high interdomain flexibility couples Rep's activities as initiators and as helicases.
External linksNucleic Acids Res / PubMed:35871290 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.96 Å
Structure data

12975

7ola

EMDB-12975, PDB-7ola:
Structure of Primase-Helicase in SaPI5
Method: EM (single particle) / Resolution: 3.3 Å

12982

7om0

EMDB-12982, PDB-7om0:
Structure of Primase-Helicase in SaPI5
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-12987: Structure of Rep protein in SaPI1
Method: EM (single particle) / Resolution: 3.9 Å

13342

7pds

EMDB-13342, PDB-7pds:
The structure of PriRep1 with dsDNA
Method: EM (single particle) / Resolution: 3.14 Å

EMDB-13945: Rep-apo
Method: EM (single particle) / Resolution: 3.96 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

Source
  • staphylococcus aureus (bacteria)
KeywordsREPLICATION / Helicase / DNA binding / AMPPNP / SaPI1

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