Unknown

Dataset Information

0

Staphylococcal self-loading helicases couple the staircase mechanism 1 with inter domain high flexibility


ABSTRACT:

SUBMITTER: Ignacio Mir Sanchis 

PROVIDER: EMPIAR-10945 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications

Staphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.

Qiao Cuncun C   Debiasi-Anders Gianluca G   Mir-Sanchis Ignacio I  

Nucleic acids research 20220801 14


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  ...[more]

Similar Datasets

| S-EPMC9371898 | biostudies-literature
| S-EPMC4040187 | biostudies-literature
| S-EPMC10844203 | biostudies-literature
| S-EPMC7132064 | biostudies-literature
| S-EPMC5356007 | biostudies-literature
| S-EPMC6900637 | biostudies-literature
| S-EPMC3261565 | biostudies-literature