Interactions between Adenylate Cyclase and the Yeast GTPase-Activating Protein IRA1
| Autor: | M R Mitts, J Bradshaw-Rouse, Warren Heideman |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Growth-hormone-releasing hormone receptor Blotting Western Molecular Sequence Data Adenylate kinase Saccharomyces cerevisiae Biology Cyclase Antibodies GTP Phosphohydrolases Fungal Proteins Muscarinic acetylcholine receptor M5 heterocyclic compounds Amino Acid Sequence Cloning Molecular Ras2 Molecular Biology Cyclase-associated protein family Cell Membrane GTPase-Activating Proteins Guanylate cyclase 2C Cell Biology Repressor Proteins Biochemistry Mutation Chromatography Gel Cyclase activity Research Article Adenylyl Cyclases |
| Zdroj: | Molecular and Cellular Biology. 11:4591-4598 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/mcb.11.9.4591-4598.1991 |
| Popis: | The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B. |
| Databáze: | OpenAIRE |
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