Premium
Primary structure of the β‐subunit of bovine transducin deduced from the cDNA sequence
Author(s) -
Sugimoto Katsunori,
Nukada Toshihide,
Tanabe Tsutomu,
Takahashi Hideo,
Noda Masaharu,
Minamino Naoto,
Kangawa Kenji,
Matsuo Hisayuki,
Hirose Tadaaki,
Inayama Seiichi,
Numa Shosaku
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80015-6
Subject(s) - transducin , complementary dna , cdna library , microbiology and biotechnology , biology , nucleic acid sequence , coding region , protein primary structure , peptide sequence , rna , biochemistry , dna , g protein , gene , receptor
DNA complementary to the bovine retinal mRNA coding for the β‐subunit of transducin has been cloned by screening a cDNA library with oligodeoxyribonucleotide probes. Nucleotide sequence analysis of the cloned cDNA has revealed that this polypeptide consists of 340 amino acid residues (including the initiating methionine). Furthermore, cDNA hybridizable with a transducin β‐subunit cDNA probe has been cloned from a library derived from bovine brain poly(A) + RNA. Comparison of the cloned cDNAs, in conjunction with blot hybridization analysis and S 1 nuclease mapping of poly(A) + RNA from bovine retina, brain and liver, suggests that the mRNAs coding for the β‐subunits of transducin and other guanine nucleotide binding proteins have the same protein‐coding sequence but partly different 5'‐noncoding sequences.