期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 75, 期 9, 页码 1613-1622出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-018-2747-6
关键词
Elongator; Transcription; tRNA modification; X-ray crystallography; Electron microscopy; Familial dysautonomia
资金
- Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery Grant [418157-2012]
- Canadian Institutes of Health Research (CIHR) Foundation Grant [FDN-143228]
- Michael Smith Foundation for Health Research Career Investigator Award
- CIHR New Investigator Award
- NSERC PGS-D fellowship
Conserved from yeast to humans, Elongator is a protein complex implicated in multiple processes including transcription regulation, alpha-tubulin acetylation, and tRNA modification, and its defects have been shown to cause human diseases such as familial dysautonomia. Elongator consists of two copies of six core subunits (Elp1, Elp2, Elp3, Elp4, Elp5, and Elp6) that are organized into two subcomplexes: Elp1/2/3 and Elp4/5/6 and form a stable assembly of similar to 850 kDa in size. Although the catalytic subunit of Elongator is Elp3, which contains a radical S-adenosyl-l-methionine (SAM) domain and a putative histone acetyltransferase domain, the Elp4/5/6 subcomplex also possesses ATP-modulated tRNA binding activity. How at the molecular level, Elongator performs its multiple functions and how the different subunits regulate Elongator's activities remains poorly understood. Here, we provide an overview of the proposed functions of Elongator and describe how recent structural studies provide new insights into the mechanism of action of this multifunctional complex.
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