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Monomeric cohesin state revealed by live‐cell single‐molecule spectroscopy
Author(s) -
Liu Wenjie,
Biton Elisheva,
Pathania Anjali,
Matityahu Avi,
Irudayaraj Joseph,
Onn Itay
Publication year - 2019
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201948211
Subject(s) - cohesin , microbiology and biotechnology , protein subunit , biology , chemistry , genetics , dna , gene , chromatin
The cohesin complex plays an important role in the maintenance of genome stability. Cohesin is composed of four core subunits and a set of regulatory subunits that interact with the core subunits. Less is known about cohesin dynamics in live cells and on the contribution of individual subunits to the overall complex. Understanding the tethering mechanism of cohesin is still a challenge, especially because the proposed mechanisms are still not conclusive. Models proposed to describe tethering depend on either the monomeric cohesin ring or a cohesin dimer. Here, we investigate the role of cohesin dynamics and stoichiometry in live yeast cells at single‐molecule resolution. We explore the effect of regulatory subunit deletion on cohesin mobility and found that depletion of different regulatory subunits has opposing effects. Finally, we show that cohesin exists mostly as a canonical monomer throughout the cell cycle, and its monomeric form is independent of its regulatory factors. Our results demonstrate that single‐molecule tools have the potential to provide new insights into the cohesin mechanism of action in live cells.