Hsp100/ClpB Chaperone Function and Mechanism

Vierling, Elizabeth¹ 

[1] University of Massachusetts

关键词: protein folding;    protein degradation;    chloroplasts;    chaperones;    protein assembly;   

DOI  :  10.2172/1168677
RP-ID  :  DOE-UMass06646
PID  :  OSTI ID: 1168677
Others  :  Other: FG02-99 ER20338

学科分类：生物科学（综合）

美国|英语

来源: SciTech Connect

【 摘 要 】

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???.