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Comparison of phosphorylation of elongation factor 1 from different species by caScin kinase II
Author(s) -
E Paleń,
Theodore T. Huang,
Jolinda A. Traugh
Publication year - 1990
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(90)81317-h
Subject(s) - phosphorylation , casein kinase 2 , serine , protein subunit , kinase , biochemistry , gtp' , threonine , protein kinase a , casein kinase 1 , biology , g alpha subunit , chemistry , microbiology and biotechnology , enzyme , cyclin dependent kinase 2 , gene
One subunit of EF‐1 or EF‐1/βγ from Artemia salina , wheat germ and rabbit reticulocytes is modified by caScin kinase II. The subunit corresponds to the low M r , subunit of EF‐1 (26000–36000) which functions along with a higher M i subunit (46000–48000). to catalyze the exchange of GDP for GTP on EF‐1α. The factor from Artemia and wheat germ is phosphorylated directly on serine by casein kinase II whereas a modulatory compound is required for phosphorylation of EF‐1 from reticulocytes. Polylysine increases the rate of phosphorylation of EF‐1 from reticulocytes by 24‐fold: both serine and threonine arc modified. This suggests that polylysinc may be substituting for a physiological regulatory compound which modulates phosphoryation in vivo.