Bovine mitochondrial rhodanese is a phosphoprotein.
The mitochondrial sulfurtransferase, rhodanese, has been analyzed for phosphate content. Significant amounts of protein-bound phosphate (30-40%) were measured in the six rhodanese preparations examined. Chromatographic experiments followed by phosphate analyses done on two of the preparations indicated that rhodanese A and rhodanese B, two enzyme forms that were previously resolved on DEAE-Sephadex by Blumenthal and Heinrikson (Blumenthal, K., and Heinrikson, R. L. (1971) J. Biol. Chem. 240, 2430-2437), correspond to dephospho- and phosphorhodanese, respectively. The phosphorylation of rhodanese by [gamma-32P]ATP is catalyzed by cAMP-dependent protein kinase. The stoichiometry of 32P incorporation based on the amount of dephosphorhodanese in the enzyme preparation approaches 1.0. The phosphorylation site is accessible in rhodanese that is free of substrate sulfur but not in the covalent enzyme-sulfur intermediate which is formed as an obligatory step during the course of catalysis. Because the cellular localization of cAMP-dependent protein kinase makes it unlikely as the physiologic modulator of rhodanese activity, liver extracts have been tested for a rhodanese kinase that does not require cAMP. Rhodanese kinase activity which is independent of cAMP is observed in extract fractions resolved by Affi-Gel Blue chromatography and freed from endogenous rhodanese by chromatography on Sephadex G-100. These results together with previous findings from this and other laboratories have led to a working model of a bicyclic cascade system that can modulate the rate of mitochondrial respiration. The essence of the model is a transduction and amplification of cellular signals into the altered covalent phosphorylation of rhodanese. Rhodanese, in turn, serves as a converter enzyme which directly alters the rate of the respiratory chain and, thus, ATP production by the reversible sulfuration of key iron-sulfur centers. The model, when expanded to include signal pathways initiated by hormones or neurotransmitters, represents a mechanism by which mitochondria can recognize and meet changing energy demands.
Ogata
K
K
Department of Biochemistry and Biophysics, John A. Burns School of Medicine, University of Hawaii, Honolulu 96822.
Dai
X
X
Volini
M
M
D000818:Animals; D002417:Cattle; D006006:Glycogen Synthase / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D008962:Models, Theoretical; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013466:Sulfurtransferases / Q000378:metabolism*; D013884:Thiosulfate Sulfurtransferase / Q000302:isolation & purification / Q000378:metabolism*
D007527:Isoenzymes; D010750:Phosphoproteins; D006006:Glycogen Synthase; D011494:Protein Kinases; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase