The same mutation in Gsalpha and transducin alpha reveals behavioral differences between these highly homologous G protein alpha-subunits.

ABSTRACT: Mutating Arg-238 to Glu (R238E) in the switch 3 region of a transducin alpha (*Talpha) in which 27 aa of the GTPase domain have been replaced with those of the alpha-subunit of the inhibitory G protein 1 (Gi1alpha), was reported to create an alpha-subunit that is resistant to activation by GTPgammaS, is devoid of resident nucleotide, and has dominant negative (DN) properties. In an attempt to create a DN stimultory G protein alpha (Gsalpha) with a single mutation we created Gsalpha-R265E, equivalent to *Talpha-R238E. Gsalpha-R265E has facilitated activation by GTPgammaS, a slightly facilitated activation by GTP but much reduced receptor plus GTP stimulated activation, and an apparently unaltered ability to interact with receptor as seen in ligand binding studies. Further, the activity prof

SUBMITTER: Zurita AR 

PROVIDER: S-EPMC2268142 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature