Grant C M, Firoozan M and Tuite M F 1989 Mistranslation induces the heat-shock response in the yeast Saccharomyces cerevisiae Mol. Gottesman S, Squires C, Pichersky E, Carrington M, Hobbs M, Mattick J S, Dalrymple B, Kuramitsu H, Shiroza T, Foster T, Clark W P, Ross B, Squires C L and Maurizi M R 1990 Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes Proc. Gottesman S and Maurizi M R 1992 Regulation by proteolysis: energy-dependent proteases and their targets Microbiol. Gottesman S, Clark W P, de Grecy-Lagard V and Maurizi M R 1993 ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli J.

Gottesman S 1989 Genetics of proteolysis in Escherichia coli Annu. 60 321–347įlanagan.J M, Wall J S, Capel M S, Schneider D K and Shanklin J 1995 Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetramer with an axial pore Biochemistry 34 10910–10917įleischmann R D, Adams M D, White O, Clayton R A, Kirkness E F, Kerlavage A R, Blut C J, Tomb J-F, Dougherty B A, Merrick J M, McKenney K, Sutton G, FitzHugh W, Fields C, Gocayne J D, Scott J, Shirley R, Liu L-I, Glodek A, Kelley J M, Weidman J F, Phillips C A, Spriggs T, Hedblom E, Cotton M D, Utterback T R, Hanna M C, Nguyen D T, Saudek D M, Brandon R C, Fine L D, Fritchman J L, Fuhrmann J L, Geoghagen N S M, Gnehm C L, McDonald L A, Small K V, Fraser C M, Smith H O and Venter J C 1995 Whole-genome random sequencing and assembly of Haemophilus influenzae Rd Science 269 496–512 26 851–862Įllis R J and Van der Vies S M 1991 Molecular chaperones Annu.

100 2081–2089Ĭlarke A K, Gustafsson P and Lidholm J Å 1994 Identification and expresion of the chloroplast clpP gene in the conifer Pinus contorta Plant Mol. This review briefly covers recent findings on the diversity of Clp proteins and their potential importance within the cell.Ĭhernoff Y O, Lindquist S L, Ono B-I, Inge-Vechtomov S G and Liebman S W 1995 Role of the chaperone protein hsp104 in propagation of the yeast prion-like factor Science 268 880–883Ĭlarke A K and Critchley C 1992 The identification of a heat-shock protein complex in chloroplasts of barley leaves Plant Physiol. The union of chaperone and proteolytic regulatory functions in one molecule suggests that certain Clp proteins play a decisive role in determining the destiny of proteins, not only during normal growth but also under conditions of extreme stress. Clp proteins presumably help to stabilize selected polypeptides during severe thermal stress and enable resolubilization of non-functional protein aggregates, as well as promoting the degradation of irreversibly damaged polypeptides. At high temperatures, additional Clp proteins are induced in response to rising levels of inactive polypeptides, resulting from either biosynthetic errors, thermal denaturation and aggregation. Constitutive Clp proteins are involved foremost in cellular protein maintenance and repair, in cooperation with other chaperone and proteolytic systems. Besides being regulators of energy-dependent proteolysis, Clp proteins may also function as molecular chaperones. The Clp/HSP1 00 protein family is a recently characterized representative, with constitutive and stress-inducible members found in many different organisms and various intracellular locations. These systems control many aspects of protein structure and function throughout the cell under all types of growth regimes. Most stress-inducible polypeptides are members of broader protein families that function either as molecular chaperones or constituents of proteolytic pathways.

Destiny chaperone