Publication Date:
1992-07-31
Description:
A genetic method, the two-hybrid system, was used to identify four genes encoding proteins that interact with the SNF1 protein kinase from yeast. One of the genes, SIP1, was independently isolated as a multicopy suppressor of defects caused by reduced SNF1 kinase activity, and genetic evidence supports its function in the SNF1 pathway. The SIP1 protein co-immunoprecipitated with SNF1 and was phosphorylated in vitro. Thus, the two-hybrid system, which is applicable to any cloned gene, can be used to detect physical interactions between protein kinases and functionally related substrate proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, X -- Hubbard, E J -- Carlson, M -- CA09503/CA/NCI NIH HHS/ -- GM34095/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):680-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Development, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496382" target="_blank"〉PubMed〈/a〉
Keywords:
AMP-Activated Protein Kinases
;
Amino Acid Sequence
;
Base Sequence
;
DNA-Binding Proteins/metabolism
;
Fungal Proteins/*genetics/*metabolism
;
Genes, Fungal
;
Molecular Sequence Data
;
Mutagenesis
;
Phosphorylation
;
Plasmids
;
Protein Kinases/*metabolism
;
*Protein-Serine-Threonine Kinases
;
Recombinant Fusion Proteins/*metabolism
;
Restriction Mapping
;
Saccharomyces cerevisiae/*enzymology
;
*Saccharomyces cerevisiae Proteins
;
Substrate Specificity
;
*Transcription Factors
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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