RGS3 is the largest member of the recently discovered family of proteins (RGS proteins) that function as negative regulators of heterotrimeric G protein signaling. Despite the intense interest in RGS proteins as physiological regulators of G protein signaling, there is little understanding of the structure and regulation of mammalian RGS genes. Using long distance PCR, we amplified and characterized the entire coding and 5'-untranslated region (5'-UTR) of the human RGS3 gene. The coding region of the human (RGS3) gene spans 14.7 kb and contains 6 exons and the 5'-UTR spans 3.2 kb and contains 2 exons. Mapping of the exons revealed that the RGS domain, conserved among all RGS proteins, was encoded by three exons, while the unique amino terminal domain of RGS3 was encoded by a single exon. The intron locations of the human RGS3 and RGS2 genes were remarkably conserved, providing the first conceptual support for a common ancestral mammalian RGS gene. 5'-RACE analysis was used to map the transcription start site 517 bp upstream of the translational start site. Analysis of 1 kb of the 5'-flanking region revealed the presence of many potential regulatory elements, the presence of an initiator (Inr) element overlapping the transcription start site, and the absence of a TATA or CCAAT box at usual positions. By radiation hybrid mapping, the human RGS3 gene was assignett to human chromosome 9q31-q33. This study is the first to elucidate the structure, chromosomal location and regulatory sequences of the RGS3 gene. (NIH HL41071, DK25295).
|Original language||English (US)|
|Publication status||Published - Dec 1 1997|
ASJC Scopus subject areas
- Molecular Biology