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Construction of a Soluble Adenylyl Cyclase Activated by G s α and Forskolin
Abstract
A soluble adenylyl cyclase was constructed by linkage of portions of the cytosolic domains of the mammalian type I and type II enzymes. The soluble enzyme was stimulated by both forskolin and the α subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) G s (G s α). Expression of the construct complemented the catabolic defect in a strain of Escherichia coli that is deficient in adenylyl cyclase activity. The active, approximately 60-kilodalton enzyme accumulated in the cytoplasmic fraction of E. coli to yield activities in excess of 1 nanomole per minute per milligram of protein. The two sets of transmembrane helices of mammalian adenylyl cyclases are thus not necessary for the catalytic or the most characteristic regulatory activities of the enzyme. This system may be useful for both genetic and biochemical analysis of G protein-regulated adenylyl cyclases.
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Cited by
Organization and Ca2+Regulation of Adenylyl Cyclases in cAMP Microdomains
Willoughby, D., & Cooper, D. M. F. (2007) · Physiological Reviews · doi:10.1152/physrev.00049.2006 · Cited by 451
Isoforms of Mammalian Adenylyl Cyclase: Multiplicities of Signaling
Sunahara, R. K. (2002) · Molecular Interventions · doi:10.1124/mi.2.3.168 · Cited by 406
The actin cytoskeleton in endothelial cell phenotypes
Prasain, N., & Stevens, T. (2009) · Microvascular Research · doi:10.1016/j.mvr.2008.09.012 · Cited by 291
Dessauer, C. W., Watts, V. J., Ostrom, R. S., Conti, M., Dove, S., & Seifert, R. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.013078 · Cited by 201
Ludwig, M.-G., & Seuwen, K. (2002) · Journal of Receptors and Signal Transduction · doi:10.1081/rrs-120014589 · Cited by 102
Metadata
- Authors
- Tang, W.-J., & Gilman, A. G.
- Venue
- Science
- Published
- 1995-06-23
- Volume
- 268
- Issue
- 5218
- Pages
- 1769-1772
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2006726587
- Cited by
- 188
- References
- 1
- FWCI
- 5.80
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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