Isolation of a cAMP receptor protein from yeast mitochondria (Mr 45000) and comparison with mitochondrial RNA polymerase (Mr 45000).
We have isolated a cAMP-binding protein from highly purified yeast mitochondria by affinity chromatography. It is a lipophilic protein of molecular mass 45 000 Da, which is tightly membrane-bound and localized on the outer surface of the inner membrane. It can be solubilized in active form under mild conditions. The cAMP receptor resembles mitochondrial RNA polymerase prepared as described by Levens et al. [(1981) J. Biol. Chem. 256, 1474] in a surprisingly large number of properties including molecular mass. Comparison of the two proteins revealed that the polypeptide previously considered as RNA polymerase is, in fact, a mitochondrial cAMP receptor protein.
Bandlow
W
W
Schwarz
U
U
Rödel
G
G
Strobel
G
G
Wachter
C
C
D002845:Chromatography; D000242:Cyclic AMP / Q000494:pharmacology; D004247:DNA / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D003902:Detergents; D007425:Intracellular Membranes / Q000032:analysis; D008928:Mitochondria / Q000032:analysis*; D008970:Molecular Weight; D011953:Receptors, Cyclic AMP / Q000302:isolation & purification* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000032:analysis*; D012995:Solubility; D014158:Transcription, Genetic / Q000187:drug effects
D003902:Detergents; D011953:Receptors, Cyclic AMP; D004247:DNA; D000242:Cyclic AMP; D012321:DNA-Directed RNA Polymerases