The primary structure of the α subunit of human elongation factor 1
Structural aspects of guanine-nucleotide-binding sites
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 155, Issue 1, pages 167–171, February 1986
How to Cite
BRANDS, J. H. G. M., MAASSEN, J. A., VAN HEMERT, F. J., AMONS, R. and MÖLLER, W. (1986), The primary structure of the α subunit of human elongation factor 1. European Journal of Biochemistry, 155: 167–171. doi: 10.1111/j.1432-1033.1986.tb09472.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received October 16, 1985) – EJB 85 1145
The primary structure of the α subunit of elongation factor 1 (EF- 1α) from human MOLT 4 cells was determined by cDNA sequencing. The data show that the conservation of the amino acid sequence is more than 80% when compared with yeast and Artemia EF-1α. An inventory of amino acid sequences around the guanine-nucleotide-binding site in elongation factor Tu from Escherichia coli and homologous amino acid sequences in G proteins, initiation and elongation factors and proteins from the RAS family shows two regions containing conserved seqence elements.
Region I has the sequence apolar-Xaa-Xaa-Xaa-Gly-Xaa-Xaa-Yaa-Xaa-Gly-Lys-Thr(Ser)-Xaa-Xaa-Xaa-Xaa-X-apolar. Except for RAS proteins, Yaa is always an acidic amino acid residue. Region II is characterized by the invariant sequence apolar-apolar-Xaa-Xaa-Asn-Lys-Xaa-Asp. In order to facilitate sequence comparison we have used a graphic display, which is based on the hydrophilicity values of individual amino acids in a sequence.