Abstract
G proteins are responsible for modulating the activity of intracellular effector systems in response to receptor activation. The stimulatory G protein Gs is responsible for activation of adenylate cyclase in response to a variety of hormonal signals. In this report, we describe the structure of the gene for the α subunit of Drosophila melanogaster Gs. The gene is approximately 4.5 kilobases long and is divided into nine exons. The exon-intron structure of the Drosophila gene shows substantial similarity to that of the human gene for Gsα. Alternate splicing of intron 7, involving either use of an unusual TG or consensus AG 3′ splice site, results in transcripts which code for either a long (DGsαL) or short (DGsαS) form of Gsα. These subunits differ by inclusion or deletion of three amino acids and substitution of a Ser for a Gly. The two forms of Drosophila Gsα differ in a region where no variation in the primary sequence of vertebrate Gsα subunits has been observed. In vitro translation experiments demonstrated that the Drosophila subunits migrate anomalously on sodium dodecyl sulfate-polyacrylamide gels with apparent molecular weights of 51,000 and 48,000. Additional Gsα transcript heterogeneity reflects the use of multiple polyadenylation sites.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 910-917 |
| Number of pages | 8 |
| Journal | Molecular and Cellular Biology |
| Volume | 10 |
| Issue number | 3 |
| State | Published - 1990 |
Fingerprint
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Two forms of drosophila melanogaster Gsα are produced by alternate splicing involving an unusual splice site. / Quan, Franklin; Forte, Michael.
In: Molecular and Cellular Biology, Vol. 10, No. 3, 1990, p. 910-917.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Two forms of drosophila melanogaster Gsα are produced by alternate splicing involving an unusual splice site
AU - Quan, Franklin
AU - Forte, Michael
PY - 1990
Y1 - 1990
N2 - G proteins are responsible for modulating the activity of intracellular effector systems in response to receptor activation. The stimulatory G protein Gs is responsible for activation of adenylate cyclase in response to a variety of hormonal signals. In this report, we describe the structure of the gene for the α subunit of Drosophila melanogaster Gs. The gene is approximately 4.5 kilobases long and is divided into nine exons. The exon-intron structure of the Drosophila gene shows substantial similarity to that of the human gene for Gsα. Alternate splicing of intron 7, involving either use of an unusual TG or consensus AG 3′ splice site, results in transcripts which code for either a long (DGsαL) or short (DGsαS) form of Gsα. These subunits differ by inclusion or deletion of three amino acids and substitution of a Ser for a Gly. The two forms of Drosophila Gsα differ in a region where no variation in the primary sequence of vertebrate Gsα subunits has been observed. In vitro translation experiments demonstrated that the Drosophila subunits migrate anomalously on sodium dodecyl sulfate-polyacrylamide gels with apparent molecular weights of 51,000 and 48,000. Additional Gsα transcript heterogeneity reflects the use of multiple polyadenylation sites.
AB - G proteins are responsible for modulating the activity of intracellular effector systems in response to receptor activation. The stimulatory G protein Gs is responsible for activation of adenylate cyclase in response to a variety of hormonal signals. In this report, we describe the structure of the gene for the α subunit of Drosophila melanogaster Gs. The gene is approximately 4.5 kilobases long and is divided into nine exons. The exon-intron structure of the Drosophila gene shows substantial similarity to that of the human gene for Gsα. Alternate splicing of intron 7, involving either use of an unusual TG or consensus AG 3′ splice site, results in transcripts which code for either a long (DGsαL) or short (DGsαS) form of Gsα. These subunits differ by inclusion or deletion of three amino acids and substitution of a Ser for a Gly. The two forms of Drosophila Gsα differ in a region where no variation in the primary sequence of vertebrate Gsα subunits has been observed. In vitro translation experiments demonstrated that the Drosophila subunits migrate anomalously on sodium dodecyl sulfate-polyacrylamide gels with apparent molecular weights of 51,000 and 48,000. Additional Gsα transcript heterogeneity reflects the use of multiple polyadenylation sites.
UR - http://www.scopus.com/inward/record.url?scp=0025037869&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025037869&partnerID=8YFLogxK
M3 - Article
C2 - 2106072
AN - SCOPUS:0025037869
VL - 10
SP - 910
EP - 917
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
SN - 0270-7306
IS - 3
ER -