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  Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

Mönkemeyer, L., Klaips, C. L., Balchin, D., Körner, R., Hartl, F. U., & Bracher, A. (2019). Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2. Molecular Cell, 74(1), 88-100.e9. doi:10.1016/j.molcel.2019.01.034.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-DD88-B Version Permalink: http://hdl.handle.net/21.11116/0000-0003-DD89-A
Genre: Journal Article

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 Creators:
Mönkemeyer, Leonie1, Author              
Klaips, Courtney L.1, Author              
Balchin, David1, Author              
Körner, Roman1, Author              
Hartl, F. Ulrich1, Author              
Bracher, Andreas1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: PHOSDUCIN-LIKE PROTEIN; SACCHAROMYCES-CEREVISIAE; IN-VIVO; CONFORMATIONAL-CHANGES; CYTOSOLIC CHAPERONIN; MOLECULAR CHAPERONE; INTERACTION NETWORK; EXCHANGE; COMPLEX; INTERACTOMEBiochemistry & Molecular Biology; Cell Biology;
 Abstract: Eukaryotic elongation factor 2 (eEF2) is an abundant and essential component of the translation machinery. The biogenesis of this 93 kDa multi-domain protein is assisted by the chaperonin TRiC/CCT. Here, we show in yeast cells that the highly conserved protein Hgh1 (FAM203 in humans) is a chaperone that cooperates with TRiC in eEF2 folding. In the absence of Hgh1, a substantial fraction of newly synthesized eEF2 is degraded or aggregates. We solved the crystal structure of Hgh1 and analyzed the interaction of wild-type and mutant Hgh1 with eEF2. These experiments revealed that Hgh1 is an armadillo repeat protein that binds to the dynamic central domain III of eEF2 via a bipartite interface. Hgh1 binding recruits TRiC to the C-terminal eEF2 module and prevents unproductive interactions of domain III, allowing efficient folding of the N-terminal GTPase module. eEF2 folding is completed upon dissociation of TRiC and Hgh1.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 74 (1) Sequence Number: - Start / End Page: 88 - 100.e9 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929