Literature DB >> 2573603

Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein.

L A Mizzen1, C Chang, J I Garrels, W J Welch.   

Abstract

We describe the identification, characterization, and purification of two members of the mammalian stress protein family, both of which are shown to be components of the mitochondria. The first, with an apparent mass of 58,000 daltons, is a constitutive protein whose synthesis increases in cells exposed to elevated temperatures and/or amino acid analogs and is therefore referred to as heat shock protein hsp 58 (hsp 58). The second, with an apparent mass of 75,000 daltons, is also a constitutive protein whose synthesis is increased in cells following glucose deprivation or exposure to either a calcium ionophore or 2-deoxyglucose and therefore represents a member of the so-called glucose-regulated proteins (grp 75). In cells treated with the potassium ionophore, nonactin, both hsp 58 and grp 75 were observed to accumulate in precursor form. Since nonactin has been reported to specifically inhibit the processing of cytoplasmic precursor proteins destined for the mitochondria, we investigated whether mature hsp 58 and grp 75 were components of the mitochondria. Mitochondria were isolated from rat liver and shown to contain both hsp 58 and grp 75. Indirect immunofluorescence using antibodies specific to either hsp 58 or grp 75 confirmed their presence within mitochondria. Proteolytic digestion experiments with intact mitochondria indicated that both proteins were not accessible to external proteolytic attack, suggesting that they are not exposed on the cytoplasmic face of the outer membrane. Based on a variety of biochemical and immunological criteria, grp 75 is shown to be a member of the hsp 70 family of stress proteins, while hsp 58 represents the mammalian equivalent of the bacterial groEL protein. Procedures for the purification of both hsp 58 and grp 75 are presented. The possible biochemical role of these two mitochondrial stress proteins is discussed in relation to the known biochemical function of their related stress protein counterparts.

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Year:  1989        PMID: 2573603

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  43 in total

Review 1.  A review of the role of 70 kDa heat shock proteins in protein translocation across membranes.

Authors:  E Craig; P J Kang; W Boorstein
Journal:  Antonie Van Leeuwenhoek       Date:  1990-10       Impact factor: 2.271

Review 2.  The human HSP70 family of chaperones: where do we stand?

Authors:  Jürgen Radons
Journal:  Cell Stress Chaperones       Date:  2016-02-10       Impact factor: 3.667

3.  The Hsp70/J-protein machinery of the African trypanosome, Trypanosoma brucei.

Authors:  Stephen John Bentley; Miebaka Jamabo; Aileen Boshoff
Journal:  Cell Stress Chaperones       Date:  2018-12-01       Impact factor: 3.667

4.  Isolation and characterization of extragenic suppressors of mutations in the SSA hsp70 genes of Saccharomyces cerevisiae.

Authors:  R J Nelson; M F Heschl; E A Craig
Journal:  Genetics       Date:  1992-06       Impact factor: 4.562

5.  Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system.

Authors:  Ohad Iosefson; Shelly Sharon; Pierre Goloubinoff; Abdussalam Azem
Journal:  Cell Stress Chaperones       Date:  2011-08-03       Impact factor: 3.667

6.  The combined effects of high temperature and carbon monoxide on heat stress response.

Authors:  T C Wu; H Z He; R M Tanguay; Y Wu; D G Xu; R W Currie; S Qu; J D Feng; G G Zhang
Journal:  J Tongji Med Univ       Date:  1995

7.  Migration of mitochondria to viral assembly sites in African swine fever virus-infected cells.

Authors:  G Rojo; M Chamorro; M L Salas; E Viñuela; J M Cuezva; J Salas
Journal:  J Virol       Date:  1998-09       Impact factor: 5.103

8.  Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family.

Authors:  S Z Domanico; D C DeNagel; J N Dahlseid; J M Green; S K Pierce
Journal:  Mol Cell Biol       Date:  1993-06       Impact factor: 4.272

9.  Expression of heat shock protein 70 is altered by age and diet at the level of transcription.

Authors:  A R Heydari; B Wu; R Takahashi; R Strong; A Richardson
Journal:  Mol Cell Biol       Date:  1993-05       Impact factor: 4.272

10.  Regulation of HSP60 mRNA expression in a human ovarian carcinoma cell line.

Authors:  E Kimura; R E Enns; F Thiebaut; S B Howell
Journal:  Cancer Chemother Pharmacol       Date:  1993       Impact factor: 3.333

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