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Regulation of adenylyl cyclase from Blastocladiella emersonii by guanine nucleotides
Author(s) -
Terenzi Hernán,
da Costa Maia José Carlos
Publication year - 1993
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(93)81669-q
Subject(s) - gs alpha subunit , adenylyl cyclase , cholera toxin , gtp' , biochemistry , adcy9 , adcy10 , g protein , cyclase , biology , protein subunit , g alpha subunit , nucleotide , chemistry , microbiology and biotechnology , enzyme , receptor , gene
GTPγS stimulates adenylyl cyclase in particulate fractions of Blastocladiella emersonii zoospores. Cholera toxin catalyses the ADP‐ribosylation of a membrane protein of a molecular weight (46,000) similar to that of the α subunit of G s found in vertebrate cells. A membrane protein of 46 kDa can also be recognized in Western blots by an antipeptide antiserum (RM/1) raised against the C‐terminus of Gα s ‐subunits. These results suggest that a G‐protein mediates the regulation of Blastocladiella adenylyl cyclase by guanine nucleotides.