Referee: Dr. Peter Csermely, Department of Medical Chemistry, Semmeliweis Univ. School of Medicine, P.O. Box 260, H-1444 Budapest 8, Hungary Hsp100/Clp family of proteins is ubiquitously distributed in living systems. Detailed work carried out in bacterial and yeast cells has shown that regulatory members of the Clp family (mainly ClpA, ClpB, and ClpC), together with the catalytic subunit (mainly ClpP), comprise an ATP-dependent two-component proteolytic system. Members of the Hsp100/Clp protein family are not only involved in the regulation of energy-dependent protein hydrolysis but also function as molecular chaperones. However, the biochemical/physiological role(s) of the Hsp100/Clp protein family in higher plants has yet to be elucidated. Recently, this protein family has been implicated in plant stress responses: the hot1 mutant of Arabidopsis thaliana , which has mutation in hsp101 gene, and is defective in tolerance to high temperature (S.-W. Hong and E. Vierling, 2000, Proc Natl Acad Sci USA , 97 (8), 4392-4397) and the transgenic Arabidopsis thaliana plants overexpressing AtHsp101 gene exhibit high temperature tolerance (C. Quietsch et al., 2000, Plant Cell , 12, 479-492). Furthermore, the Hsp101 protein is involved in the translational regulation of cellular mRNAs and one such candidate has been identified as the photosynthetic electron transport gene Ferredoxin 1 mRNA (J. Ling et al., 2000, Plant Cell , 12, 1213-1227). We present what is known about the bacterial, yeast, and plant Hsp100/Clp proteins, discuss their possible relationship, and, more importantly, examine the cellular roles that this important family of proteins plays in plants.
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Document Type: Research Article
Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi 110021, INDIA
Department of Biochemistry, University of California, Riverside, California 92521-0129 USA.
Publication date: May 1, 2001