Comparison of phosphorylation of elongation factor 1 from different species by caScin kinase II
- 12 November 1990
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 274 (1-2) , 12-14
- https://doi.org/10.1016/0014-5793(90)81317-h
Abstract
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 Mr, subunit of EF-1 (26000–36000) which functions along with a higher Mi 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 vivoKeywords
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