Immunological and molecular characterization of Go alpha-like proteins in the Drosophila central nervous system

J Biol Chem. 1989 Nov 5;264(31):18552-60.

Abstract

The alpha subunits of heterotrimeric G proteins are responsible for the coupling of receptors for a wide variety of stimuli to a number of intracellular effector systems. In the nervous system of vertebrates, high levels of a specific class of G protein (Go alpha) are expressed. The alpha subunit of Go serves as a substrate for modification by pertussis toxin (PTX). In this report, we demonstrate that the Drosophila heads contain high levels of a 40-kDa PTX substrate. Modification of this protein by PTX is modulated in a manner similar to that observed for vertebrate G proteins. The PTX substrate in Drosophila is also recognized specifically by antibodies raised against peptide sequences found specifically in vertebrate Go alpha. Vertebrate Go alpha probes were used to identify a Drosophila cDNA coding for a potential PTX substrate with high sequence identity (82%) to vertebrate Go alpha. An additional cDNA coding for a related Go alpha has also been isolated. The two cDNAs differ only in the 5'-untranslated and amino-terminal regions of the protein. This observation, in addition to Northern analysis, suggests that alternate splicing may generate a variety of Go alpha-like proteins in Drosophila. In situ hybridization of specific probes to tissue sections indicates that the mRNAs coding for Go alpha-like proteins in Drosophila are expressed primarily in neuronal cell bodies and, at lower levels, in the eyes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Western
  • Chromosome Mapping
  • DNA / genetics
  • DNA / isolation & purification
  • DNA Probes
  • Drosophila melanogaster / analysis*
  • GTP-Binding Proteins / analysis*
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism
  • Gene Expression
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Guanosine Triphosphate / pharmacology
  • Immunosorbent Techniques
  • Molecular Sequence Data
  • Nervous System / analysis*
  • Nucleic Acid Hybridization
  • Pertussis Toxin*
  • Sequence Homology, Nucleic Acid
  • Thionucleotides / pharmacology
  • Virulence Factors, Bordetella / metabolism*

Substances

  • DNA Probes
  • Thionucleotides
  • Virulence Factors, Bordetella
  • Adenosine Diphosphate Ribose
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Guanosine Triphosphate
  • DNA
  • Pertussis Toxin
  • GTP-Binding Proteins

Associated data

  • GENBANK/J05089