Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function.
Protein homeostasis relies on the accurate translation and folding of newly synthesized proteins. Eukaryotic elongation factor 2 (eEF2) promotes GTP-dependent translocation of the ribosome during translation. eEF2 folding was recently shown to be dependent on Hsp90 as well as the cochaperones Hgh1,...
Saved in:
Main Authors: | Melody D Fulton, Danielle J Yama, Ella Dahl, Jill L Johnson |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2024-12-01
|
Series: | PLoS Genetics |
Online Access: | https://doi.org/10.1371/journal.pgen.1011508 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.
by: Rebecca Mercier, et al.
Published: (2023-05-01) -
A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A
by: Ibrahim M. Sabbarini, et al.
Published: (2025-02-01) -
The known unknowns of the Hsp90 chaperone
by: Laura-Marie Silbermann, et al.
Published: (2024-12-01) -
Identification and expression analysis of the heat shock proteins Hsp70, Hsp90, and Hsp90b in Litopenaeus vannamei under low-temperature stress
by: Min Peng, et al.
Published: (2025-03-01) -
Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy
by: Tjaša Goričan, et al.
Published: (2024-12-01)