Author:
Rumyantseva Natalya A.,Shutov Vladimir M.,Belenkaia Dina G.,Alekseev Aleksandr A.,Morozova Natalia E.,Vedyaykin Alexey D.
Abstract
AbstractSMC (Structural Maintenance of Chromosomes) ATPase proteins are integral components of complexes bearing the same name, crucial for the spatial organization of DNA across diverse life forms, spanning bacteria, archaea, and eukaryotes. It is proposed that in bacteria, SMC complexes facilitate DNA compaction through loop extrusion and aid in the segregation of daughter nucleoids. In this paper the properties of the SMC ATPase protein fromUreaplasma parvumwere investigated by using a spectrum of methods, including conventional biochemical methods as well as advanced single-molecule techniques. Our findings reveal distinctive properties of this protein compared to its extensively studied homologue fromBacillus subtilis. Notably, our results suggest thatU. parvumSMC ATPase facilitates DNA compaction even in the absence of ATP.
Publisher
Cold Spring Harbor Laboratory