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

doi:10.1016/j.cub.2010.12.004

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 journal › Article › peer-review

137 Citations (Scopus)

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.

Original language	English
Pages (from-to)	12-24
Number of pages	12
Journal	Current Biology
Volume	21
Issue number	1
DOIs	https://doi.org/10.1016/j.cub.2010.12.004
Publication status	Published - 11 Jan 2011

Bibliographical 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.

Data Availability Statement

All data have been deposited in the National Center for Biotechnology Information Sequence Read Archive database (http://trace.ncbi.nlm.nih.gov/Traces/sra/) with the accession number SRP004703.

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Cite this

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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.",

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AU - Hu, Bin

AU - Itoh, Takehiko

AU - Mishra, Ajay

AU - Katoh, Yuki

AU - Chan, Kok-Lung

AU - Upcher, William

AU - Godlee, Camilla

AU - Roig, Maurici B.

AU - Shirahige, Katsuhiko

AU - Nasmyth, Kim

N1 - 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.

PY - 2011/1/11

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N2 - 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.

AB - 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.

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DO - 10.1016/j.cub.2010.12.004

M3 - Article

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JO - Current Biology

JF - Current Biology

IS - 1

ER -

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

Abstract

Bibliographical note

Data Availability Statement

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