scholarly journals Mitochondrial proteome disruption in the diabetic heart through targeted epigenetic regulation at the mitochondrial heat shock protein 70 (mtHsp70) nuclear locus

2018 ◽  
Vol 119 ◽  
pp. 104-115 ◽  
Author(s):  
Danielle L. Shepherd ◽  
Quincy A. Hathaway ◽  
Cody E. Nichols ◽  
Andrya J. Durr ◽  
Mark V. Pinti ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Epigenetic Regulation ◽  
Heat Shock Protein 70 ◽  
Diabetic Heart ◽  
Mitochondrial Proteome ◽  
Nuclear Locus ◽  
Mitochondrial Heat Shock Protein

Characterization and expression analysis of a mitochondrial heat-shock protein 70 gene from the Antarctic moss Pohlia nutans

Polar Biology ◽  
2014 ◽  
Vol 37 (8) ◽  
pp. 1145-1155 ◽  
Author(s):  
Shenghao Liu ◽  
Jing Wang ◽  
Bailin Cong ◽  
Xiaohang Huang ◽  
Kaoshan Chen ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Expression Analysis ◽  
Heat Shock Protein 70 ◽  
Mitochondrial Heat Shock Protein ◽  
The Antarctic ◽  
Pohlia Nutans ◽  
Antarctic Moss

scholarly journals The Life Span Determinant p66Shc Localizes to Mitochondria Where It Associates with Mitochondrial Heat Shock Protein 70 and Regulates Trans-membrane Potential

2004 ◽  
Vol 279 (24) ◽  
pp. 25689-25695 ◽  
Author(s):  
Francesca Orsini ◽  
Enrica Migliaccio ◽  
Maurizio Moroni ◽  
Cristina Contursi ◽  
Veronica A. Raker ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Life Span ◽  
Heat Shock Protein 70 ◽  
Mitochondrial Heat Shock Protein

scholarly journals Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA.

1994 ◽  
Vol 127 (4) ◽  
pp. 893-902 ◽  
Author(s):  
J M Herrmann ◽  
R A Stuart ◽  
E A Craig ◽  
W Neupert
Keyword(s):  
Mitochondrial Dna ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Critical Role ◽  
Molecular Complexes ◽  
Mitochondrial Ribosomes ◽  
Mitochondrial Heat Shock Protein

Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix. Here, we describe a role for mt-Hsp70 in chaperoning proteins encoded by mitochondrial DNA and synthesized within mitochondria. The availability of mt-Hsp70 function influences the pattern of proteins synthesized in mitochondria of yeast both in vivo and in vitro. In particular, we show that mt-Hsp70 acts in maintaining the var1 protein, the only mitochondrially encoded subunit of mitochondrial ribosomes, in an assembly competent state, especially under heat stress conditions. Furthermore, mt-Hsp70 helps to facilitate assembly of mitochondrially encoded subunits of the ATP synthase complex. By interacting with the ATP-ase 9 oligomer, mt-Hsp70 promotes assembly of ATP-ase 6, and thereby protects the latter protein from proteolytic degradation. Thus mt-Hsp70 by acting as a chaperone for proteins encoded by the mitochondrial DNA, has a critical role in the assembly of supra-molecular complexes.

scholarly journals Cloning and Expression of Mitochondrial Heat Shock Protein 70 of Trypanosoma congolense and Potential Use as a Diagnostic Antigen

2003 ◽  
Vol 10 (5) ◽  
pp. 926-933 ◽  
Author(s):  
Hiroshi Bannai ◽  
Tatsuya Sakurai ◽  
Noboru Inoue ◽  
Chihiro Sugimoto ◽  
Ikuo Igarashi
Keyword(s):  
Amino Acids ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cdna Clone ◽  
Heat Shock Protein 70 ◽  
Trypanosoma Congolense ◽  
Cloning And Expression ◽  
Antibody Detection ◽  
Diagnostic Antigen ◽  
Mitochondrial Heat Shock Protein

ABSTRACT The ability to use mitochondrial heat shock protein 70 (MTP) of Trypanosoma congolense as a diagnostic antigen was examined. One cDNA clone was obtained by immunoscreening of a T. congolense procyclic form (PCF) cDNA library with monoclonal antibody (MAb) 10F9. The cDNA clone contained an open reading frame of 1,977 bp encoding a polypeptide consisting of 659 amino acids. Southern blotting analysis indicated that there were at least three copies of the MTP gene in the haploid genome. Interference of the MTP RNA resulted in complete inhibition, which indicated that MTP is essential at the PCF stage. Northern and Western blotting analyses revealed that MTP is expressed both in the bloodstream form (BSF) and in PCF. The B-cell epitope recognized by MAb 10F9 was located within 206 amino acids from the C terminus. Depending on the conditions of protein extraction, MTP was cleaved into smaller polypeptides by endogenous proteases. However, the C-terminal epitope of MTP was preserved with a high degree of antigenicity, even after cleavage. Antibody detection by enzyme-linked immunosorbent assay with the truncated recombinant MTP revealed that anti-MTP antibodies exist in experimentally infected mouse sera. Thus, MTP may be useful as an antigen for the serodiagnosis of primary T. congolense infection.

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