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Molecular cloning and sequence determination of a cDNA coding for the α‐subunit of a G o ‐type protein of Xenopus laevis oocytes
Author(s) -
Olate Juan,
Jorquera Hugo,
Purcell Patricia,
Codina Juan,
Birnbaumer Lutz,
Allende Jorge E.
Publication year - 1989
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(89)81190-1
Subject(s) - xenopus , complementary dna , biology , microbiology and biotechnology , protein subunit , cdna library , g alpha subunit , peptide sequence , coding region , oligonucleotide , molecular cloning , amino acid , homology (biology) , cloning (programming) , dna , genetics , gene , computer science , programming language
Xenopus laevis oocytes are cells ideally suited to the study of signal transduction and of the G‐proteins that are involved in this process. A X. laevis cDNA library in λgt10 has been screened with a mixture of three oligonucleotide probes designed to detect sequences found in various mammalian α‐subunits of G‐proteins. One of these clones has been purified through tertiary screening and the DNA insert has been sequenced. This clone was found to include the total sequence coding for a 354 amino acid protein that is 89% identical to the sequence of α‐subunit of rat G o . The differences with the mammalian protein were clustered in amino acids 290–315, which have been postulated to define the region interacting with the receptor and effector molecule. The homology with the α‐subunits of other mammalian G‐proteins is lower (65–70% to G i and 42% to G s ). On this basis, this clone can be classified as G o ‐like.