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TitleMolecular architecture of the yeast Elongator complex reveals an unexpected asymmetric subunit arrangement.
Journal, issue, pagesEMBO Rep, Vol. 18, Issue 2, Page 280-291, Year 2017
Publish dateNov 21, 2016
AuthorsDheva T Setiaputra / Derrick Th Cheng / Shan Lu / Jesse M Hansen / Udit Dalwadi / Cindy Hy Lam / Jeffrey L To / Meng-Qiu Dong / Calvin K Yip /
PubMed AbstractElongator is a ~850 kDa protein complex involved in multiple processes from transcription to tRNA modification. Conserved from yeast to humans, Elongator is assembled from two copies of six unique ...Elongator is a ~850 kDa protein complex involved in multiple processes from transcription to tRNA modification. Conserved from yeast to humans, Elongator is assembled from two copies of six unique subunits (Elp1 to Elp6). Despite the wealth of structural data on the individual subunits, the overall architecture and subunit organization of the full Elongator and the molecular mechanisms of how it exerts its multiple activities remain unclear. Using single-particle electron microscopy (EM), we revealed that yeast Elongator adopts a bilobal architecture and an unexpected asymmetric subunit arrangement resulting from the hexameric Elp456 subassembly anchored to one of the two Elp123 lobes that form the structural scaffold. By integrating the EM data with available subunit crystal structures and restraints generated from cross-linking coupled to mass spectrometry, we constructed a multiscale molecular model that showed the two Elp3, the main catalytic subunit, are located in two distinct environments. This work provides the first structural insights into Elongator and a framework to understand the molecular basis of its multifunctionality.
External linksEMBO Rep / PubMed:27872205 / PubMed Central
MethodsEM (single particle)
Resolution24.1 - 25.2 Å
Structure data

EMDB-8239:
EM map of the intact yeast Elongator complex
Method: EM (single particle) / Resolution: 25.2 Å

EMDB-8291:
EM map of the Elp123 subcomplex of yeast Elongator
Method: EM (single particle) / Resolution: 24.1 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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