Detection of the peptidyltransferase activity of a dipeptide, alanylhistidine, in the absence of ribosomes.

Abstract:

:It was shown that a dipeptide, alanylhistidine, can act as a catalyst for the peptidyl transfer reaction in the absence of ribosomes between the amino acid moieties of phenylalanyl, lysyl, prolyl, and glycyl tRNAs depending on their model templates, poly U, poly A, poly C, and poly G, respectively. A template effect was observed: The peptidyl transfer reaction between tRNAGly molecules (anticodon GCC) occurred in the presence of poly G but not in the presence of poly C. The reaction was most efficient for the best stacked poly A (tRNALys) and least efficient for the worst stacked poly U (tRNAPhe).

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Shimizu M

doi

10.1093/oxfordjournals.jbchem.a021318

subject

Has Abstract

pub_date

1996-05-01 00:00:00

pages

832-4

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

119

pub_type

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