ATP hydrolysis is required for relocating cohesin from sites occupied by its Scc2/4 loading complex

Bin Hu, Takehiko Itoh, Ajay Mishra, Yuki Katoh, Kok-Lung Chan, William Upcher, Camilla Godlee, Maurici B. Roig, Katsuhiko Shirahige, Kim Nasmyth

Research output: Contribution to journalArticlepeer-review

137 Citations (Scopus)


The Cohesin complex that holds sister chromatins together until anaphase is comprised of three core subunits: Smc1 and Smc3, two long-rod-shaped proteins with an ABC-like ATPase head (nucleotide-binding domain [NBD]) and a dimerization domain linked by a 50 nm long intramolecular antiparallel coiled-coil, and Scc1, an α-kleisin subunit interconnecting the NBD domains of Smc1 and Smc3. Cohesin's stable association with chromosomes is thought to involve entrapment of chromatin fibers by its tripartite Smc1-Smc3-Scc1 ring via a poorly understood mechanism dependent on a separate Scc2/4 loading complex. A key issue concerns where entrapment initially takes place: at sites where cohesin is found stably associated or at distinct "loading" sites from which it translocates.
Original languageEnglish
Pages (from-to)12-24
Number of pages12
JournalCurrent Biology
Issue number1
Publication statusPublished - 11 Jan 2011

Bibliographical note

We are grateful to Nasmyth lab members for useful discussions, R. Parton for help with microscopy, K. Nakagawa for ChIP-SEQ, B. Panaretou and K. Bloom for providing useful yeast strains and plasmids, and S. Gruber for critical reading of the manuscript. T.I. and Y.K. were supported by Grant-in-Aid for Young Scientists (A) from MEXT. K.S. was supported by a grant of the Cell Innovation Program and Grant-in-Aid for Scientific Research (S) from the MEXT, Japan. K.N. was supported by Cancer Research UK and the Wellcome Trust.

Data Availability Statement

All data have been deposited in the National Center for Biotechnology Information Sequence Read Archive database ( with the accession number SRP004703.


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