Cellular and Molecular Life Sciences

, Volume 75, Issue 9, pp 1613–1622 | Cite as

Structural insights into the function of Elongator

  • Udit Dalwadi
  • Calvin K. Yip


Conserved from yeast to humans, Elongator is a protein complex implicated in multiple processes including transcription regulation, α-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 ~ 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.


Elongator Transcription tRNA modification X-ray crystallography Electron microscopy Familial dysautonomia 



Adenosine triphosphate


Coenzyme A




Cryo electron microscopy


Elongator protein


Electron microscopy


Familial dysautonomia


Guanine-nucleotide exchange factor


Gcn5-related N-terminal acetyltransferase


Histone acetyltransferase


IκB kinase associated protein


Inhibitor of kappa light polypeptide gene enhancer in B cells, kinase complex-associated protein


Insensitive to killer toxin-3


Inhibitor of kappa-B








RNA polymerase II




Tetratricopeptide repeat


Typtophan-aspartic acid-40



This work was supported by a Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery Grant (418157-2012), a Canadian Institutes of Health Research (CIHR) Foundation Grant (FDN-143228), a Michael Smith Foundation for Health Research Career Investigator Award, a CIHR New Investigator Award to CY, and an NSERC PGS-D fellowship to U.D.


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© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyThe University of British ColumbiaVancouverCanada

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