@article{6d6da9597d5f4ae993bb8d7d5c515381,
title = "ATP hydrolysis is required for relocating cohesin from sites occupied by its Scc2/4 loading complex",
abstract = "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.",
author = "Bin Hu and Takehiko Itoh and Ajay Mishra and Yuki Katoh and Kok-Lung Chan and William Upcher and Camilla Godlee and Roig, {Maurici B.} and Katsuhiko Shirahige and Kim Nasmyth",
note = "Acknowledgments 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.",
year = "2011",
month = jan,
day = "11",
doi = "10.1016/j.cub.2010.12.004",
language = "English",
volume = "21",
pages = "12--24",
journal = "Current Biology",
issn = "0960-9822",
publisher = "Cell Press",
number = "1",
}