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Literature DB >> 8098536

Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.

Abstract

Two families of molecular chaperone, the hsp 60-GroEL family and the TF55-TCP1 family, have been discovered in evolutionarily related cellular compartments. A member of one of these families, hsp 60, has been shown to play a global role in polypeptide chain folding in mitochondria. We review here studies of both hsp 60 and other family members, discussing their essential physiological roles and mechanism of action.

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Year: 1993 PMID： 8098536 DOI： 10.1098/rstb.1993.0030

Source DB: PubMed Journal: Philos Trans R Soc Lond B Biol Sci ISSN： 0962-8436 Impact factor: 6.237

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Cited

23 in total

1. Myelin-associated glycoprotein gene mutation causes Pelizaeus-Merzbacher disease-like disorder.

Authors: Alexander Lossos; Nimrod Elazar; Israela Lerer; Ora Schueler-Furman; Yakov Fellig; Benjamin Glick; Bat-El Zimmerman; Haim Azulay; Shlomo Dotan; Sharon Goldberg; John M Gomori; Penina Ponger; J P Newman; Hodaifah Marreed; Andreas J Steck; Nicole Schaeren-Wiemers; Nofar Mor; Michal Harel; Tamar Geiger; Yael Eshed-Eisenbach; Vardiella Meiner; Elior Peles
Journal: Brain Date: 2015-07-15 Impact factor: 13.501

2. Novel isolation method and structural stability of a eukaryotic chaperonin: the TCP-1 ring complex from rabbit reticulocytes.

Authors: M T Norcum
Journal: Protein Sci Date: 1996-07 Impact factor: 6.725

Review 3. Molecular chaperones and protein folding in plants.

Authors: R S Boston; P V Viitanen; E Vierling
Journal: Plant Mol Biol Date: 1996-10 Impact factor: 4.076

4. Artificial Fusion of mCherry Enhances Trehalose Transferase Solubility and Stability.

Authors: Luuk Mestrom; Stefan R Marsden; Marit Dieters; Puck Achterberg; Lysanne Stolk; Isabel Bento; Ulf Hanefeld; Peter-Leon Hagedoorn
Journal: Appl Environ Microbiol Date: 2019-04-04 Impact factor: 4.792

5. Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta.

Authors: D Miklos; S Caplan; D Mertens; G Hynes; Z Pitluk; Y Kashi; K Harrison-Lavoie; S Stevenson; C Brown; B Barrell
Journal: Proc Natl Acad Sci U S A Date: 1994-03-29 Impact factor: 11.205

6. A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

Authors: B P Burnett; A L Horwich; K B Low
Journal: J Bacteriol Date: 1994-11 Impact factor: 3.490

Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.

1. Myelin-associated glycoprotein gene mutation causes Pelizaeus-Merzbacher disease-like disorder.

2. Novel isolation method and structural stability of a eukaryotic chaperonin: the TCP-1 ring complex from rabbit reticulocytes.

Review 3. Molecular chaperones and protein folding in plants.

4. Artificial Fusion of mCherry Enhances Trehalose Transferase Solubility and Stability.

5. Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta.

6. A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

7. The Tcp-1-related gene, Cctg, maps to mouse chromosome 3.

8. Expression of Heat Shock Protein 70 in Human Skin Cells as a Photoprotective Function after UV Exposure.

9. Intracellular localization of a group II chaperonin indicates a membrane-related function.

10. Heat-inducible proteins that react with antibodies to chaperonin60 are localized in the nucleus of a fish cell line.