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Molecular characterization of a membrane‐bound cGMP dependent protein kinase from the silk moth Bombyx mori
Author(s) -
Tanoue S.,
Nishioka T.
Publication year - 2003
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2003.00448.x
Subject(s) - biology , bombyx mori , protein kinase a , cyclic nucleotide gated ion channel , microbiology and biotechnology , signal transduction , biochemistry , kinase , midgut , biophysics , gene , cyclic nucleotide , botany , nucleotide , larva
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‐Iα and BmPKG‐Iβ. The deduced amino acid sequences indicate that both BmPKG‐Iα and BmPKG‐Iβ appear to consist of an amino terminal region, a cGMP binding domain and a protein kinase domain. Transcripts of BmPKG‐Iα and BmPKG‐Iβ were detected in various tissues: flight muscles, antennae, midgut, legs, head, thoracic ganglia and Malphighian tubules. Recombinant BmPKG‐Iα bound to lipid membranes, while BmPKG‐Iα with a deleted amino terminal region failed to bind to lipid membranes.