Label-free electrochemical monitoring of DNA ligase activity [PDF]
, 2008 This study presents a simple, label-free electrochemical technique for the monitoring of DNA ligase activity. DNA ligases are enzymes that catalyze joining of breaks in the backbone of DNA and are of significant scientific interest due to their essential
Ahel I. +29 more
core +1 more source
Direct comparison of nick-joining activity of the nucleic acid ligases from bacteriophage T4 [PDF]
, 2006 The genome of bacteriophage T4 encodes three polynucleotide ligases, which seal the backbone of nucleic acids during infection of host bacteria. The T4Dnl (T4 DNA ligase) and two RNA ligases [T4Rnl1 (T4 RNA ligase 1) and T4Rnl2] join a diverse array of ...
Amitsur +61 more
core +4 more sources
Analysis of ligation and DNA binding by Escherichia coli DNA ligase (LigA). [PDF]
, 2005 NAD+-dependent DNA ligases are essential enzymes in bacteria, with the most widely studied of this class of enzymes being LigA from Escherichia coli. NAD+-dependent DNA ligases comprise several discrete structural domains, including a BRCT domain at the ...
Adam Wilkinson +59 more
core +1 more source
Mammalian DNA ligases. Catalytic domain and size of DNA ligase I. [PDF]
Journal of Biological Chemistry, 1990 DNA ligase I is the major DNA ligase activity in proliferating mammalian cells. The protein has been purified to apparent homogeneity from calf thymus. It has a monomeric structure and a blocked N-terminal residue. DNA ligase I is a 125-kDa polypeptide as estimated by sodium dodecyl sulfate-gel electrophoresis and by gel chromatography under denaturing
Dana D. Lasko +3 more
openaire +2 more sources
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
core +2 more sources
Characterization of a temperature-sensitive DNA ligase from Escherichia coli [PDF]
, 2004 DNA ligases are essential enzymes in cells due to their ability to join DNA strand breaks formed during DNA replication. Several temperature-sensitive mutant strains of Escherichia coli, including strain GR501, have been described which can be ...
Bowater, Laura +8 more
core +1 more source
Evaluation of NAD(+)-dependent DNA ligase of mycobacteria as a potential target for antibiotics [PDF]
, 2007 Mycobacteria contain genes for several DNA ligases, including ligA, which encodes a NAD+-dependent enzyme that has been postulated to be a target for novel antibacterial compounds.
Bowater, Richard P. +6 more
core +2 more sources
NAD+-dependent DNA ligases of Mycobacterium tuberculosis and Streptomyces coelicolor [PDF]
, 2003 Sequencing of the genomes of Mycobacterium tuberculosis H37Rv and Streptomyces coelicolor A3(2) identified putative genes for an NAD+-dependent DNA ligase. We have cloned both open reading frames and overexpressed the protein products in Escherichia coli.
Bowater, Richard +6 more
core +1 more source
The role of Schizosaccharomyces pombe SUMO ligases in genome stability [PDF]
, 2007 SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is ...
A. Skilton +44 more
core +2 more sources
The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]
, 2018 Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren +4 more
core +1 more source