Molecular characterization of a membrane-bound cGMP dependent protein kinase from the silk moth Bombyx mori

Insect Mol Biol. 2003 Dec;12(6):621-9. doi: 10.1046/j.1365-2583.2003.00448.x.

Abstract

The cGMP signalling pathway has been suggested to be involved in the signal transduction of various physiological functions in insects; olfaction, antidiuresis and eclosion. However, the cGMP signalling mechanism has remained elusive. We isolated two cDNAs of the cGMP dependent protein kinase, designated BmPKG-Ialpha and BmPKG-Ibeta. The deduced amino acid sequences indicate that both BmPKG-Ialpha and BmPKG-Ibeta appear to consist of an amino terminal region, a cGMP binding domain and a protein kinase domain. Transcripts of BmPKG-Ialpha and BmPKG-Ibeta were detected in various tissues: flight muscles, antennae, midgut, legs, head, thoracic ganglia and Malphighian tubules. Recombinant BmPKG-Ialpha bound to lipid membranes, while BmPKG-Ialpha with a deleted amino terminal region failed to bind to lipid membranes.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Western
  • Bombyx / enzymology*
  • Bombyx / genetics*
  • Cell Membrane / metabolism
  • Cells, Cultured
  • Cyclic GMP-Dependent Protein Kinases / genetics*
  • Cyclic GMP-Dependent Protein Kinases / isolation & purification
  • Cyclic GMP-Dependent Protein Kinases / metabolism
  • DNA Primers
  • DNA, Complementary / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression*
  • Molecular Sequence Data
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Analysis, DNA

Substances

  • DNA Primers
  • DNA, Complementary
  • Cyclic GMP-Dependent Protein Kinases