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Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I)Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I)
Structural highlights
FunctionSMC4_YEAST Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Publication Abstract from PubMedSignificanceDNA needs to be compacted to fit into nuclei and during cell division, when dense chromatids are formed for their mechanical segregation, a process that depends on the protein complex condensin. It forms and enlarges loops in DNA through loop extrusion. Our work resolves the atomic structure of a DNA-bound state of condensin in which ATP has not been hydrolyzed. The DNA is clamped within a compartment that has been reported previously in other structural maintenance of chromosomes (SMC) complexes, including Rad50, cohesin, and MukBEF. With the caveat of important differences, it means that all SMC complexes cycle through at least some similar states and undergo similar conformational changes in their head modules, while hydrolyzing ATP and translocating DNA. Clamping of DNA shuts the condensin neck gate.,Lee BG, Rhodes J, Lowe J Proc Natl Acad Sci U S A. 2022 Apr 5;119(14):e2120006119. doi: , 10.1073/pnas.2120006119. Epub 2022 Mar 29. PMID:35349345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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