期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:2005
卷号:102
期号:17
页码:6108-6113
DOI:10.1073/pnas.0502270102
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:G protein-mediated signaling is implicated in yeast and fungal cAMP pathways. By two-hybrid screens and pull-down experiments, we show that the fission yeast Gpa2 G binds an N-terminal domain of adenylate cyclase, comprising a moderately conserved sequence within a region otherwise poorly related to other fungal adenylate cyclases. Overexpressing this domain in yeast perturbs cAMP signaling, which is restored by Gpa2 coexpression. Mutations affecting this domain, over 1,100 residues from the catalytic domain, alter glucose-triggered cAMP signaling. This is evidence for direct activation of adenylate cyclase by a fungal G protein and suggests a distinct activation mechanism from that of mammals.