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J. Biol. Chem., Vol. 278, Issue 20, 17601-17608, May 16, 2003
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From the Molecular Biology Program, Sloan-Kettering Institute,
New York, New York 10021
Bacteriophage T4 RNA ligase 2 (Rnl2) exemplifies
a polynucleotide ligase family that includes the trypanosome
RNA-editing ligases and putative RNA ligases encoded by eukaryotic
viruses and archaea. Here we analyzed 12 individual amino acids of Rnl2 that were identified by alanine scanning as essential for strand joining. We determined structure-activity relationships via
conservative substitutions and examined mutational effects on the
isolated steps of ligase adenylylation and phosphodiester bond
formation. The essential residues of Rnl2 are located within conserved
motifs that define a superfamily of nucleotidyl transferases that act via enzyme-(lysyl-N)-NMP intermediates. Our mutagenesis results underscore a shared active site architecture in Rnl2-like ligases, DNA
ligases, and mRNA capping enzymes. They also highlight two essential signature residues, Glu34 and
Asn40, that flank the active site lysine nucleophile
(Lys35) and are unique to the Rnl2-like ligase family.
Structure-Function Analysis of T4 RNA Ligase 2*
*
This work was supported by National Institutes of Health
Grant GM63611.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Fax:
212-717-3623; E-mail: s-shuman@ski.mskcc.org.
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