Characterization of an ATP-dependent DNA ligase encoded by haemophilus influenzae Journal Article
| Authors: | Cheng, C.; Shuman, S. |
| Article Title: | Characterization of an ATP-dependent DNA ligase encoded by haemophilus influenzae |
| Abstract: | We report that Haemophilus influenzae encodes a 268 amino acid ATP-dependent DNA ligase. The specificity of Haemophilus DNA ligase was investigated using recombinant protein produced in Escherichia coli. The enzyme catalyzed efficient strand joining on a singly nicked DNA in the presence of magnesium and ATP (K(m) = 0.2 μM). Other nucleoside triphosphates or deoxynucleoside triphosphates could not substitute for ATP. Haemophilus ligase reacted with ATP in the absence of DNA substrate to form a covalent ligaseadenylate intermediate. This nucleotidyl transferase reaction required a divalent cation and was specific for ATP. The Haemophilus enzyme is the first example of an ATP-dependent DNA ligase encoded by a eubacterial genome. It is also the smallest member of the covalent nucleotidyl transferase superfamily, which includes the bacteriophage and eukaryotic ATP-dependent polynucleotide ligases and the GTP-dependent RNA capping enzymes. |
| Keywords: | controlled study; nonhuman; animal cell; dna repair; enzyme activity; bacteria (microorganisms); animalia; dna; amino acid sequence; molecular sequence data; eukaryota; escherichia coli; recombinant proteins; substrate specificity; recombinant protein; adenosine triphosphate; polydeoxyribonucleotide synthase; enzyme specificity; enzyme substrate complex; protein dna interaction; dna ligases; magnesium ion; divalent cation; adenine; adenosine phosphate; nucleotidyltransferase; magnesium; bacterial enzyme; open reading frames; haemophilus; haemophilus influenzae; priority journal; article |
| Journal Title: | Nucleic Acids Research |
| Volume: | 25 |
| Issue: | 7 |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Date Published: | 1997-04-01 |
| Start Page: | 1369 |
| End Page: | 1374 |
| Language: | English |
| DOI: | 10.1093/nar/25.7.1369 |
| PUBMED: | 9060431 |
| PROVIDER: | scopus |
| PMCID: | PMC146593 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 17 March 2017 -- Source: Scopus |
