Characterization of Agrobacterium tumefaciens DNA ligases C and D Journal Article
| Authors: | Zhu, H.; Shuman, S. |
| Article Title: | Characterization of Agrobacterium tumefaciens DNA ligases C and D |
| Abstract: | Agrobacterium tumefaciens encodes a single NAD+-dependent DNA ligase and six putative ATP-dependent ligases. Two of the ligases are homologs of LigD, a bacterial enzyme that catalyzes end-healing and end-sealing steps during nonhomologous end joining (NHEJ). Agrobacterium LigD1 and AtuLigD2 are composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3′-phosphoesterase (PE) module. Both LigD proteins seal DNA nicks, albeit inefficiently. The LigD2 POL domain adds ribonucleotides or deoxyribonucleotides to a DNA primer-template, with rNTPs being the preferred substrates. The LigD1 POL domain has no detectable polymerase activity. The PE domains catalyze metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3′-terminal diribonucleotide to yield a primer-template with a monoribonucleotide 3′-OH end. The PE domains also have a 3′-phosphatase activity on an all-DNA primer-template that yields a 3′-OH DNA end. Agrobacterium ligases C2 and C3 are composed of a minimal ligase core domain, analogous to Mycobacterium LigC (another NHEJ ligase), and they display feeble nick-sealing activity. Ligation at DNA double-strand breaks in vitro by LigD2, LigC2 and LigC3 is stimulated by bacterial Ku, consistent with their proposed function in NHEJ. © 2007 The Author(s). |
| Keywords: | controlled study; unclassified drug; nonhuman; protein domain; protein function; metabolism; dna repair; in vitro study; enzymology; enzyme activity; enzyme substrate; bacteria (microorganisms); dna strand breakage; bacterial protein; chemistry; bacterial proteins; nucleotide sequence; dna breaks, double-stranded; double stranded dna break; protein structure, tertiary; 3' untranslated region; catalysis; ku antigen; polydeoxyribonucleotide synthase; mycobacterium; protein tertiary structure; dna ligases; ligase; bacterial genetics; dna template; polydeoxyribonucleotide synthase (atp); rhizobium radiobacter; polydeoxyribonucleotide synthase d; polydeoxyribonucleotide synthase c; polydeoxyribonucleotide synthase c2; polydeoxyribonucleotide synthase c3; polydeoxyribonucleotide synthase d2; agrobacterium; agrobacterium tumefaciens |
| Journal Title: | Nucleic Acids Research |
| Volume: | 35 |
| Issue: | 11 |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Date Published: | 2007-06-01 |
| Start Page: | 3631 |
| End Page: | 3645 |
| Language: | English |
| DOI: | 10.1093/nar/gkm145 |
| PUBMED: | 17488851 |
| PROVIDER: | scopus |
| PMCID: | PMC1920237 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 12" - "Export Date: 17 November 2011" - "CODEN: NARHA" - "Molecular Sequence Numbers: GENBANK: NC_002516;" - "Source: Scopus" |
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