Identification of bdm-1, a gene involved in G protein beta-subunit function and alpha-subunit accumulation.

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TitleIdentification of bdm-1, a gene involved in G protein beta-subunit function and alpha-subunit accumulation.
Publication TypeJournal Article
Year of Publication2000
AuthorsKasahara, S, Wang, P, Nuss, DL
JournalProc Natl Acad Sci U S A
Date Published2000 Jan 4
KeywordsAmino Acid Sequence, Ascomycota, Cloning, Molecular, Eye Proteins, Fungal Proteins, Genetic Complementation Test, GTP-Binding Protein alpha Subunits, Gi-Go, GTP-Binding Protein Regulators, GTP-Binding Proteins, Heterotrimeric GTP-Binding Proteins, Molecular Sequence Data, Mutation, Phenotype, Phosphoproteins, Proteins, Restriction Mapping, RNA, Messenger, Sequence Alignment, Signal Transduction, Virulence

Targeted disruption of Galpha and Gbeta genes has established the requirement of an intact G protein signaling pathway for optimal execution of several important physiological processes, including pathogenesis, in the chestnut blight fungus Cryphonectria parasitica. We now report the identification of a G protein signal transduction component, beta disruption mimic factor-1, BDM-1. Disruption of the corresponding gene, bdm-1, resulted in a phenotype indistinguishable from that previously observed after disruption of the Gbeta subunit gene, cpgb-1. The BDM-1 deduced amino acid sequence contained several significant clusters of identity with mammalian phosducin, including a domain corresponding to a highly conserved 11-amino acid stretch that has been implicated in binding to the Gbetagamma dimer and two regions of defined Gbeta/phosducin contact points. Unlike the negative regulatory function proposed for mammalian phosducin, the genetic data presented in this report suggest that BDM-1 is required for or facilitates Gbeta function. Moreover, disruption of either bdm-1 or cpgb-1 resulted in a significant, posttranscriptional reduction in the accumulation of CPG-1, a key Galpha subunit required for a range of vital physiological processes.

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID10618432
PubMed Central IDPMC26677
Grant ListGM55981 / GM / NIGMS NIH HHS / United States