\"Tissue\" transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. (Articolo in rivista)

Type
Label
  • \"Tissue\" transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbabio.2006.07.007 (literal)
Alternative label
  • Mastroberardino PG, Farrace MG, Viti I, Pavone F, Fimia GM, Melino G, Rodolfo C, Piacentini M (2006)
    "Tissue" transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes.
    in Biochimica et biophysica acta (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Mastroberardino PG, Farrace MG, Viti I, Pavone F, Fimia GM, Melino G, Rodolfo C, Piacentini M (literal)
Pagina inizio
  • 1357 (literal)
Pagina fine
  • 1365 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Mitochondria: from Molecular Insight to Physiology and Pathology (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1757 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 9-10 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biology, University of Rome “Tor Vergata”, Roma, Italy; CNR, Istituto di Neuroscienze, Sezione di Roma, Roma, Italy; Medical Research Council, Toxicology Unit, Hodgkin bld, Leicester, UK; Laboratory of Cell Biology and E.M., INMI-IRCCS “Lazzaro Spallanzani”, Roma, Italy (literal)
Titolo
  • \"Tissue\" transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. (literal)
Abstract
  • In this study we provide the first in vivo evidences showing that, under physiological conditions, \"tissue\" transglutaminase (TG2) might acts as a protein disulphide isomerase (PDI) and through this activity contributes to the correct assembly of the respiratory chain complexes. Mice lacking TG2 exhibit mitochondrial energy production impairment, evidenced by decreased ATP levels after physical challenge. This defect is phenotypically reflected in a dramatic decrease of motor behaviour of the animals. We propose that the molecular mechanism, underlying such a phenotype, resides in a defective disulphide bonds formation in ATP synthase (complex V), NADH-ubiquinone oxidoreductase (complex I), succinate-ubiquinone oxidoreductase (complex II) and cytochrome c oxidase (complex IV). In addition, TG2-PDI might control the respiratory chain by modulating the formation of the prohibitin complexes. These data elucidate a new pathway that directly links the TG2-PDI enzymatic activity with the regulation of mitochondrial respiratory chain function. (literal)
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