Identification of Nsp100 as elongation factor 2 (EF‐2)
- 14 August 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 253 (1-2) , 55-58
- https://doi.org/10.1016/0014-5793(89)80928-7
Abstract
The nerve growth factor‐sensitive phosphoprotein from PC12 cells, previously designated Nsp100, has been shown to be elongation factor 2 (EF‐2). The criteria used for this identification include: (i) similarity of N‐terminal sequence; (ii) phosphorylation by the same kinase; (iii) ADP‐ribosylation mediated by diphtheria toxin; (iv) comparable function in cell‐free protein synthesis. According to these criteria, Nsp 100 and EF‐2 are identical and the kinase that phosphorylates Nsp100 in PC12 cells is calcium/calmodulin kinase III.Keywords
This publication has 14 references indexed in Scilit:
- Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translationNature, 1988
- cAMP‐dependent activation of protein synthesis correlates with dephosphorylation of elongation factor 2FEBS Letters, 1988
- Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2.Journal of Biological Chemistry, 1987
- Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins.Proceedings of the National Academy of Sciences, 1986
- Protein kinase C as a component of a nerve growth factor-sensitive phosphorylation system in PC12 cells.Proceedings of the National Academy of Sciences, 1986
- Specific purification of elongation factor 2 and isolation of its antibodyBiochemical and Biophysical Research Communications, 1986
- Distribution of Nsp100 and Nsp100 Kinase, a Nerve Growth Factor?Sensitive Phosphorylation System, in Rat TissuesJournal of Neurochemistry, 1985
- Nerve growth factor mediates phosphorylation of specific proteinsCell, 1980
- Diphtheria ToxinAnnual Review of Biochemistry, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970