Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2.
A cDNA clone, pHGR81, encoding 358 amino-acid residues of the C-terminal region of human elongation factor 2 (EF-2), was isolated from a human ovarian granulosa cell cDNA library. The deduced amino-acid sequence of pHGR81, when compared with the known identical amino-acid sequences of hamster as well as rat EF-2 revealed a substitution of a glutamine by an alanine residue in the partially determined human sequence. The 15 amino-acid-residue sequence comprising the histidine-715, supposed to be of importance for the biological function of EF-2, is preserved in human EF-2. The coding region of the cDNA insert of pHGR81 displays a homology of 87% to hamster and of 88% to rat EF-2 cDNA. In Northern-transfer analysis, pHGR81 specifically hybridizes with an mRNA species of 3.1 kb.
Rapp
G
G
Max-Planck-Institute für Biophysikalische Chemie, Abt. Molekulare Biologie, Göttingen.
Mucha
J
J
Einspanier
R
R
Luck
M
M
Scheit
K H
KH
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D004262:DNA Restriction Enzymes; D005260:Female; D005796:Genes; D006107:Granulosa Cells / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009710:Nucleotide Mapping; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000235:genetics*
D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D004247:DNA; D004262:DNA Restriction Enzymes