Open AccessClamping of DNA shuts the condensin neck gate
Author(s) -
Byung-Gil Lee,
James Rhodes,
Jan Löwe
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2120006119
Subject(s) - condensin , cohesin , dna , biophysics , atp hydrolysis , microbiology and biotechnology , chromosome segregation , chromatid , mitosis , chemistry , biology , genetics , chromatin , chromosome , biochemistry , atpase , gene , enzyme
Significance DNA 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.