期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 67, 期 -, 页码 78-85出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2020.08.010
关键词
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资金
- Spanish Ministry of Science, Innovation and Universities (MCIU/AEI) [SAF2017-82632-P]
- European Regional Development Fund (ERDF)
- National Institute of Health Carlos III
- Autonomous Region of Madrid [Y2018/BIO4747, P2018/NMT4443]
- European Regional Development Fund
- Human Frontiers Science Project (HFSP) [RGP0031/2017]
- Autonomous Region of Madrid Attraction of Research Talent program [2018-T2/BMD-10584]
- European Social Fund
RUVBL1 and RUVBL2 are highly conserved AAA+ ATPases that form a hetero-hexameric complex involved in various cellular processes. Recent cryo-EM studies have provided insights into their role in complex protein-protein interactions.
RUVBL1 and RUVBL2 are two highly conserved AAA+ ATPases that form a hetero-hexameric complex that participates in a wide range of unrelated cellular processes, including chromatin remodeling, Fanconi Anemia (FA), nonsense-mediated mRNA decay (NMD), and assembly and maturation of several large macromolecular complexes such as RNA polymerases, the box C/D small nucleolar ribonucleoprotein (snoRNP) and mTOR complexes. How the RUVBL1-RUVBL2 complex works in such a variety of processes, sometimes antagonistic, has been obscure for a long time. Recent cryo-electron microscopy (cryo-EM) studies have started to reveal how RUVBL1- RUVBL2 forms a scaffold for complex protein-protein interactions and how the structure and ATPase activity of RUVBL1-RUVBL2 can be affected and regulated by the interaction with clients.
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