Isolation of a cAMP Receptor Protein from Yeast Mitochondria(Mr45000) and Comparison with Mitochondrial RNA Polymerase(Mr45000)
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm3.1985.366.1.545/pdf
Reference15 articles.
1. Purification of mitochondrial RNA polymerase from Saccharomyces cerevisiae.
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3. Interconvertible Enzyme Cascades in Cellular Regulation
4. Cyclic 3′,5′-adenosine monophosphate stimulates trehalose degradation in baker's yeast
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1. Transcription of the yeast mitochondrial genome requires cyclic AMP;Molecular and General Genetics MGG;1993-10
2. Two lipid-anchored cAMP-binding proteins in the yeast Saccharomyces cerevisiae are unrelated to the R subunit of cytoplasmic protein kinase A;European Journal of Biochemistry;1991-12
3. An amphitropic cAMP-binding protein in yeast mitochondria. 3. Membrane release requires both calcium-dependent phosphorylation of the cAMP-binding protein and a phospholipid-activated mitochondrial phospholipase;Biochemistry;1989-12
4. Protein phosphorylation in yeast mitochondria: cAMP-Dependence, submitochondrial localization and substrates of mitochondrial protein kinases;Yeast;1987-09
5. Isolation and characterization of a mitochondrial RNA polymerase from Drosophila melanogaster;Biochemistry and Cell Biology;1987-02-01
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