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PMID: 3882425 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Location of the adenylylation site in T4 RNA ligase.

European journal of biochemistry ·Vol. 147 ·No. 2 ·1985-03-01 ·Pages 325-9

Thøgersen HC, Morris HR, Rand KN, Gait MJ

Abstract

The purification of the enzyme T4 RNA ligase is described from an Escherichia coli strain, KR54, in which the RNA ligase gene (g63) has been inserted into the plasmid pDR540 for inducible expression of g63 from the tac promoter. Adenylylation of the purified enzyme with [14C]rATP followed by digestion with chymotrypsin yielded an adenylylated peptide, the identity of which was determined by fast-atom-bombardment mass spectrometric analysis. The results show that the AMP residue is bound covalently to the lysine at position 99 of the RNA ligase protein sequence.

MeSH Terms
Binding Sites Chymotrypsin Escherichia coli/genetics Mass Spectrometry Peptides/metabolism Polynucleotide Ligases/metabolism RNA Ligase (ATP)/genetics,metabolism T-Phages/enzymology Transformation, Bacterial
Chemicals
Peptides Chymotrypsin Polynucleotide Ligases RNA Ligase (ATP)
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Thøgersen H C
Morris H R
Rand K N
Gait M J
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1985-03-01
Pages
325-9
Language
English
Region
England
NLM ID
0107600
Subset
IM
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