Results 71 to 80 of about 54,630 (258)

Tankyrases Promote Homologous Recombination and Check Point Activation in Response to DSBs.

open access: yesPLoS Genetics, 2016
DNA lesions are sensed by a network of proteins that trigger the DNA damage response (DDR), a signaling cascade that acts to delay cell cycle progression and initiate DNA repair.
Zita Nagy   +5 more
doaj   +1 more source

Mammalian DNA ligases. Biosynthesis and intracellular localization of DNA ligase I.

open access: yesJournal of Biological Chemistry, 1990
Mammalian DNA ligase I is presumed to act in DNA replication. Rabbit antibodies against the homogeneous enzyme from calf thymus inhibited DNA ligase I activity and consistently recognized a single polypeptide of 125 kDa when cells from an established bovine kidney cell line (MDBK) were lysed rapidly by a variety of procedures and subjected to ...
D D, Lasko, A E, Tomkinson, T, Lindahl
openaire   +2 more sources

Purification and preparation of Marchantia polymorpha Auxin Response Factor 2 for phase separation studies

open access: yesFEBS Open Bio, EarlyView.
We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen   +5 more
wiley   +1 more source

MDC1 mediates Pellino recruitment to sites of DNA double-strand breaks

open access: yesLife Science Alliance
RING E3 ubiquitin ligases Pellino 1 and 2 are recruited to sites of DNA damage via their non-canonical FHA domains that recognise conserved phosphorylated sequence motifs in the DNA damage adaptor protein MDC1.
Mònica Torres Esteban   +7 more
doaj   +1 more source

The STUbL RNF4 regulates protein group SUMOylation by targeting the SUMO conjugation machinery

open access: yesNature Communications, 2017
SUMO and ubiquitin are key signal transducers in several cellular processes including the DNA-damage response. Here the authors describe a method for selective enrichment of ubiquitin substrates for E3 ligases from complex cellular proteomes and identify
Ramesh Kumar   +4 more
doaj   +1 more source

Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum

open access: yesFEBS Open Bio, EarlyView.
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey   +4 more
wiley   +1 more source

Comparative analysis of T4 DNA ligases and DNA polymerases used in chromosome conformation capture assays

open access: yesBioTechniques, 2015
Three-dimensional (3-D) genome organization in the nuclear space affects various genomic functions. Circular chromosome conformation capture (4C-seq) is a powerful technique that allows researchers to measure long-range chromosomal interactions with a ...
Michal Schwartz   +7 more
doaj   +1 more source

Mammalian DNA ligases. Catalytic domain and size of DNA ligase I.

open access: yesJournal 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
A E, Tomkinson   +3 more
openaire   +2 more sources

Threonine 348 regulates the subcellular localization of PTEN

open access: yesFEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues

open access: yesNature Communications, 2019
The DNA ligase of African swine fever virus is one of the most error-prone ligases identified to date, but underlying molecular details are lacking. Here, Chen et al.
Yiqing Chen   +13 more
doaj   +1 more source

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