A second NAD+-dependent DNA ligase (LigB) in Escherichia coli Journal Article
| Authors: | Sriskanda, V.; Shuman, S. |
| Article Title: | A second NAD+-dependent DNA ligase (LigB) in Escherichia coli |
| 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 (126KxDG) abolished nick joining and ligase-adenylate formation by LigB, thus confirming that the ligase and adenylyltransferase activities are intrinsic to the LigB protein. |
| Keywords: | controlled study; sequence analysis; mutation; nonhuman; protein function; protein motif; amino acid substitution; carboxy terminal sequence; brca1 protein; bacteria (microorganisms); amino acid sequence; molecular sequence data; sequence homology, amino acid; enzyme analysis; nucleotide sequence; escherichia coli; recombinant protein; base sequence; molecular interaction; alanine; catalysis; sequence homology; zinc; polydeoxyribonucleotide synthase; bacterial dna; dna, bacterial; lysine; cysteine; dna nick translation; isoenzymes; nicotinamide adenine dinucleotide; dna ligases; ligase; adenosine phosphate; covalent bond; negibacteria; priority journal; article |
| Journal Title: | Nucleic Acids Research |
| Volume: | 29 |
| Issue: | 24 |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Date Published: | 2001-12-15 |
| Start Page: | 4930 |
| End Page: | 4934 |
| Language: | English |
| PUBMED: | 11812821 |
| PROVIDER: | scopus |
| PMCID: | PMC97608 |
| DOI: | 10.1093/nar/29.24.4930 |
| DOI/URL: | |
| Notes: | Export Date: 21 May 2015 -- Source: Scopus |
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