skip to main content

SciTech ConnectSciTech Connect

Title: Hsp100/ClpB Chaperone Function and Mechanism

The supported research investigated the mechanism of action of a unique class of molecular chaperones in higher plants, the Hsp100/ClpB proteins, with the ultimate goal of defining how these chaperones influence plant growth, development, stress tolerance and productivity. Molecular chaperones are essential effectors of cellular “protein quality control”, which comprises processes that ensure the proper folding, localization, activation and turnover of proteins. Hsp100/ClpB proteins are required for temperature acclimation in plants, optimal seed yield, and proper chloroplast development. The model plant Arabidopsis thaliana and genetic and molecular approaches were used to investigate two of the three members of the Hsp100/ClpB proteins in plants, cytosolic AtHsp101 and chloroplast-localized AtClpB-p. Investigating the chaperone activity of the Hsp100/ClpB proteins addresses DOE goals in that this activity impacts how “plants generate and assemble components” as well as “allowing for their self repair”. Additionally, Hsp100/ClpB protein function in plants is directly required for optimal “utilization of biological energy” and is involved in “mechanisms that control the architecture of energy transduction systems”.
Authors:
 [1]
  1. Univ. of Massachusetts, Amherst, MA (United States). Dept. of Biochemistry and Molecular Biology
Publication Date:
OSTI Identifier:
1168677
Report Number(s):
DOE--UMass06646
FG02-99 ER20338
DOE Contract Number:
SC0006646; FG02-99ER20338
Resource Type:
Technical Report
Research Org:
Univ. of Massachusetts, Amherst, MA (United States)
Sponsoring Org:
USDOE Office of Science (SC)
Contributing Orgs:
Univ. of Arizona, Tucson, AZ (United States); Univ. of Pittsburgh, PA (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES protein folding; protein degradation; chloroplasts; chaperones; protein assembly