Multiple forms of Go.alpha. mRNA: analysis of the 3'-untranslated regions

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Abstract
Go, a guanine nucleotide binding protein found predominantly in neural tisues, interacts in vitro with rhodopsin, muscarinic, and other receptors and has been implicated in the regulation of ion channels. Despite the virtual identity of reported cDNA sequences for the .alpha. subunit of Go (Go.alpha.), multiple molecular weight forms of mRNA have been identified in tissues from all species examined. To investigate the molecular basis for the size heterogeneity of Go.alpha. mRNAs, four cDNA clones were isolated from the same retinal .lambda.gt10 cDNA library that was used earlier to isolate .lambda.GO9, a clone encompassing the complete coding region of Go.alpha.. These clones were identified as Go.alpha. clones based on nucleotide sequence identity with .lambda.GO9 in the coding region; they diverge, however, from .lambda.GO9 in the 3''-untranslated region 28 nucleotides past the stop codon. An oligonucleotide probe complementary to a portion of the 3''-untranslated region of .lambda.GO9 that differs from the newly isolated clones hybridized with 3.0- and 4.0-kb mRNAs present in bovine brain and retina whereas a similar probe for the unique region of the new clones hybridized with a 4.0-kb mRNA in both tissues and with a 2.0-kb mRNA found predominantly in retina. A similar hybridization pattern was observed when brain poly(A+) RNA from other species was hybridized with the different 3''-untranslated region probes. It appears that differences in the 3''-untranslated regions could, in part, be the basis for the observed heterogeneity in Go.alpha. mRNAs.

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