Limited cleavage of eucaryotic elongation factor Tu by trypsin: alignment of the tryptic fragments and effect of nucleic acids on the enzymatic reaction

Treatment of eucaryotic elongation factor Tu (eEF-Tu; M sub(r) 53000) with trypsin in the presence of 25% (v/v) glycerol results in cleavage of the factor at two sites and generates a single polypeptide of 43000 daltons termed eEF-Tu super(t) and low molecular weight peptide fragments. Treatment of...

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Bibliographic Details
Published in:Biochemistry (Easton) 1983-04, Vol.22 (8), p.1911-1917
Main Authors: Slobin, L I, Clark, R V, Olson, M O
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
elongation factor 2
eukaryotes
Molecular Weight
Peptide Elongation Factor Tu
Peptide Elongation Factors
Peptide Fragments - analysis
Rabbits
Reticulocytes - analysis
rRNA 28S
trypsin
Trypsin - metabolism
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Summary:Treatment of eucaryotic elongation factor Tu (eEF-Tu; M sub(r) 53000) with trypsin in the presence of 25% (v/v) glycerol results in cleavage of the factor at two sites and generates a single polypeptide of 43000 daltons termed eEF-Tu super(t) and low molecular weight peptide fragments. Treatment of eEF-Tu in the presence of 28S rRNA markedly accelerates the rate of trypsin cleavage of the factor, whereas treatment of eEF-Tu in the presence of 28S rRNA and in the absence of glycerol stabilizes eEF-Tu super(t) against trypsin cleavage. By contrast, cleavage of eEF-Tu by trypsin is strongly inhibited by the presence of aminoacyl-tRNA and GTP in reaction mixtures. The results, when combined with additional structural information, suggest that the aminoacyl-tRNA binding stie of eEF-Tu is located at the amino-terminal end of the factor.
ISSN:0006-2960
DOI:10.1021/bi00277a027