ATP-dependent peptide release from mitochondria of reticulocytes.
ATP-dependent release of TCA-precipitable peptides from mitochondria-containing stroma (MCS) is described. The process is independent of ubiquitin, but is sensitive to hemin and to heat treatment. Neither chloramphenicol nor EGTA inhibit. 50% of the activity is dependent on charged tRNA. The peptides released from MCS possess a molecular mass of about 1-5 kDa and are degraded to TCA-soluble compounds by a cytosolic protease system (fraction II) without ubiquitin.
Dubiel
W
W
Institute of Biochemistry, Humboldt University Berlin, GDR.
Drung
I
I
Müller
M
M
Rapoport
S M
SM
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002850:Chromatography, Gel; D006868:Hydrolysis; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000187:drug effects / Q000378:metabolism*; D014452:Ubiquitins / Q000494:pharmacology
D010455:Peptides; D014452:Ubiquitins; D000255:Adenosine Triphosphate