Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein

Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein

Redundant functions maintained from single to multi-cellular organisms have made Saccharomyces cere-visiae an important model for the analysis of con-served com-plex cellular processes. Yeast has been especially useful in understanding the regulation and function of the essential molecular chaperone...

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Bibliographic Details
Main Authors: Abbey D. Zuehlke, Leonard Neckers
Format: Article
Language:English
Published: Shared Science Publishers OG 2017-08-01
Series:Microbial Cell
Subjects:
co-chaperone
posttranslational modification
ATPase cycle
client protein
Online Access:http://microbialcell.com/researcharticles/out-with-the-old-hsp90-finds-amino-acid-residue-more-useful-than-co-chaperone-protein/
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spelling doaj-32dff5d1a80e483494e12ad0e5ecc4112020-11-24T21:43:13ZengShared Science Publishers OGMicrobial Cell2311-26382017-08-014827327410.15698/mic2017.08.586Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone proteinAbbey D. Zuehlke0Leonard Neckers1Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.Redundant functions maintained from single to multi-cellular organisms have made Saccharomyces cere-visiae an important model for the analysis of con-served com-plex cellular processes. Yeast has been especially useful in understanding the regulation and function of the essential molecular chaperone, Heat Shock Protein 90 (Hsp90). Research focused on Hsp90 has determined that it is highly regulated by both co-chaperones and posttranslational modifications. A recent study per-formed by (Zuehlke et al., 2017) demonstrates that the function of one co-chaperone in yeast is replaced by posttranslational modification (PTM) of a single amino acid within Hsp90 in higher eukaryotes.http://microbialcell.com/researcharticles/out-with-the-old-hsp90-finds-amino-acid-residue-more-useful-than-co-chaperone-protein/co-chaperoneposttranslational modificationATPase cycleclient protein
collection DOAJ
language English
format Article
sources DOAJ
author Abbey D. Zuehlke
Leonard Neckers
spellingShingle Abbey D. Zuehlke
Leonard Neckers
Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
Microbial Cell
co-chaperone
posttranslational modification
ATPase cycle
client protein
author_facet Abbey D. Zuehlke
Leonard Neckers
author_sort Abbey D. Zuehlke
title Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
title_short Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
title_full Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
title_fullStr Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
title_full_unstemmed Out with the old: Hsp90 finds amino acid residue more useful than co-chaperone protein
title_sort out with the old: hsp90 finds amino acid residue more useful than co-chaperone protein
publisher Shared Science Publishers OG
series Microbial Cell
issn 2311-2638
publishDate 2017-08-01
description Redundant functions maintained from single to multi-cellular organisms have made Saccharomyces cere-visiae an important model for the analysis of con-served com-plex cellular processes. Yeast has been especially useful in understanding the regulation and function of the essential molecular chaperone, Heat Shock Protein 90 (Hsp90). Research focused on Hsp90 has determined that it is highly regulated by both co-chaperones and posttranslational modifications. A recent study per-formed by (Zuehlke et al., 2017) demonstrates that the function of one co-chaperone in yeast is replaced by posttranslational modification (PTM) of a single amino acid within Hsp90 in higher eukaryotes.
topic co-chaperone
posttranslational modification
ATPase cycle
client protein
url http://microbialcell.com/researcharticles/out-with-the-old-hsp90-finds-amino-acid-residue-more-useful-than-co-chaperone-protein/
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