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• W146534847 abstract "Research Article1 February 1991free access Identification of regulatory residues of the yeast adenylyl cyclase. G. Feger G. Feger Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author E. De Vendittis E. De Vendittis Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author A. Vitelli A. Vitelli Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author P. Masturzo P. Masturzo Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author R. Zahn R. Zahn Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author A. C. Verrotti A. C. Verrotti Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author C. Kavounis C. Kavounis Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author G. P. Pal G. P. Pal Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author O. Fasano O. Fasano Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author G. Feger G. Feger Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author E. De Vendittis E. De Vendittis Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author A. Vitelli A. Vitelli Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author P. Masturzo P. Masturzo Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author R. Zahn R. Zahn Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author A. C. Verrotti A. C. Verrotti Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author C. Kavounis C. Kavounis Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author G. P. Pal G. P. Pal Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author O. Fasano O. Fasano Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author Author Information G. Feger1, E. De Vendittis1, A. Vitelli1, P. Masturzo1, R. Zahn1, A. C. Verrotti1, C. Kavounis1, G. P. Pal1 and O. Fasano1 1Differentiation Structures Programme, European Molecular Biology Laboratory, Heidelberg, FRG. The EMBO Journal (1991)10:349-359https://doi.org/10.1002/j.1460-2075.1991.tb07956.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We have attempted to identify amino acid residues of the yeast adenylyl cyclase that are involved in the regulation of its activity, by isolating adenylyl cyclase-linked spontaneous mutations capable of suppressing the temperature-sensitive phenotype of ras1- ras2-ts1 strains. We previously identified a mutated adenylyl cyclase in which a single point mutation, called CR14, led to the replacement of threonine 1651 with isoleucine. We have now investigated the biological effects of CR14, and of other mutations that cause the replacement of threonine 1651 by distinct amino acids. We have observed that the response of adenylyl cyclase to Ras can be either enhanced or attenuated, without significant effects on the steady-state level of the former enzyme in vivo, depending on the amino acid side chain at position 1651. Therefore, this residue identifies a regulatory region on the adenylyl cyclase molecule. We have also taken advantage of the attenuation of adenylyl cyclase function caused by the replacement of threonine 1651 with aspartic acid to isolate intragenic suppressor mutations. We have identified several point mutations, leading to single amino acid substitutions, individually capable of reactivating the attenuated adenylyl cyclase. The corresponding amino acid changes are located within a relatively small region, including residues 1331, 1345, 1348 and 1374. This region could be physiologically involved in the negative control of the carboxy-terminal catalytic domain. Previous ArticleNext Article Volume 10Issue 21 February 1991In this issue RelatedDetailsLoading ..." @default.
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• W146534847 date "1991-02-01" @default.
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• W146534847 title "Identification of regulatory residues of the yeast adenylyl cyclase." @default.
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• W146534847 doi "https://doi.org/10.1002/j.1460-2075.1991.tb07956.x" @default.
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