In Vivo Evidence for ATPase-Dependent DNA Translocation by the Bacillus subtilis SMC Condensin Complex.
Structural maintenance of chromosomes (SMC) complexes shape the genomes of virtually all organisms, but how they function remains incompletely understood. Recent studies in bacteria and eukaryotes have led to a unifying model in which these ring-shaped ATPases act along contiguous DNA segments, processively enlarging DNA loops. In support of this model, single-molecule imaging experiments indicate that Saccharomyces cerevisiae condensin complexes can extrude DNA loops in an ATP-hydrolysis-dependent manner in vitro. Here, using time-resolved high-throughput chromosome conformation capture (Hi-C), we investigate the interplay between ATPase activity of the Bacillus subtilis SMC complex and loop formation in vivo. We show that point mutants in the SMC nucleotide-binding domain that impair but do not eliminate ATPase activity not only exhibit delays in de novo loop formation but also have reduced rates of processive loop enlargement. These data provide in vivo evidence that SMC complexes function as loop extruders.
['Wang|Xindan|X|', 'Hughes|Anna C|AC|', 'Brandão|Hugo B|HB|', 'Walker|Benjamin|B|', 'Lierz|Carrie|C|', 'Cochran|Jared C|JC|', 'Oakley|Martha G|MG|', 'Kruse|Andrew C|AC|', 'Rudner|David Z|DZ|']
D000251:Adenosine Triphosphatases D000255:Adenosine Triphosphate D001412:Bacillus subtilis D001426:Bacterial Proteins D002876:Chromosomes, Bacterial D004247:DNA D004268:DNA-Binding Proteins D006868:Hydrolysis D046912:Multiprotein Complexes D017354:Point Mutation D011485:Protein Binding D012441:Saccharomyces cerevisiae D000072760:Single Molecule Imaging D014178:Translocation, Genetic
SMC condensin ParB TAD cohesin loop extrusion