Literature summary for 6.5.1.B1 extracted from

Arn, E.A.; Abelson, J.N.
The 2'-5' RNA ligase of Escherichia coli. Purification, cloning, and genomic disruption (1996), J. Biol. Chem., 271, 31145-31153.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli. Moderate overexpression of the ligase protein lead to slower growth rates and a temperature-sensitive phenotype in both wild-type and RNA ligase knockout strains	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
19930	-	calculated from sequence	Escherichia coli
20000	-	SDS-PAGE	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P37025	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3'-half-tRNA molecule with a 5'-OH end + 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end	the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+. The enzyme from Escherichia coli specifically ligates tRNA half-molecules (from Saccharomyces cerevisiae) containing nucleoside base modifications forming a 2'-5' phosphodiester bond at the ligated junction and shows a preference among different tRNA species, reversible in vitro. Yeast extract-modified pre-tRNATyr are the most active substrates tested for ligation by the Escherichia coli RNA ligase. tRNAPhe half-molecules produced by digestion of T7-transcribed pre-tRNAPhe with Saccharomyces cerevisiae tRNA splicing endonuclease are poorly ligated in Escherichia coli extracts	Escherichia coli	mature tRNA molecule containing a 2'-5'-phosphodiester bond	-	r
additional information	the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo	Escherichia coli	?	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.8	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
additional information	the enzyme does not require a nucleoside triphosphate cofactor	Escherichia coli

General Information

General Information	Comment	Organism
malfunction	cells lacking ligase activity grew normally under laboratory conditions	Escherichia coli
physiological function	the enzyme is involved in bacterial RNA processing	Escherichia coli

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Release 2023.1 (January 2023)