PMID:11812821
| Citation |
Sriskanda, V and Shuman, S (2001) A second NAD(+)-dependent DNA ligase (LigB) in Escherichia coli. Nucleic Acids Res. 29:4930-4 |
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| Abstract |
Escherichia coli DNA ligase (LigA) is the prototype of the NAD(+)-dependent class of DNA ligases found in all bacteria. Here we report the characterization of E.coli LigB, a second NAD(+)-dependent DNA ligase identified by virtue of its sequence similarity to LigA. LigB differs from LigA in that it lacks the BRCA1 C-terminus domain (BRCT) and two of the four Zn-binding cysteines that are present in LigA and all other bacterial NAD(+) ligases. We found that recombinant LigB catalyzed strand joining on a singly-nicked DNA in the presence of a divalent cation and NAD(+), and that LigB reacted with NAD(+) to form a covalent ligase-adenylate intermediate. Alanine substitution for the motif I lysine ((126)KxDG) abolished nick joining and ligase-adenylate formation by LigB, thus confirming that the ligase and adenylyltransferase activities are intrinsic to the LigB protein. |
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| Keywords |
Alanine/genetics; Amino Acid Sequence; Amino Acid Substitution; Base Sequence; DNA Ligases/genetics; DNA Ligases/isolation & purification; DNA Ligases/metabolism; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Isoenzymes/genetics; Isoenzymes/isolation & purification; Isoenzymes/metabolism; Lysine/genetics; Molecular Sequence Data; Mutation; Sequence Homology, Amino Acid |
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