Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins.
about
A DNA topoisomerase IB in Thaumarchaeota testifies for the presence of this enzyme in the last common ancestor of Archaea and EucaryaEvolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerasesGenome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the ArchaeaPrimPol, an archaic primase/polymerase operating in human cellsAn exosome-like complex in Sulfolobus solfataricus.Mechanism and evolution of DNA primasesA novel firmicute protein family related to the actinobacterial resuscitation-promoting factors by non-orthologous domain displacementOrigin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new membersThe 5S rRNA maturase, ribonuclease M5, is a Toprim domain family memberMechanisms for initiating cellular DNA replicationStructures to complement the archaeo-eukaryotic primases catalytic cycle description: What's next?Urzymology: experimental access to a key transition in the appearance of enzymesStructure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution.Crystal structure and mutational study of RecOR provide insight into its mode of DNA bindingHoloenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VICrystal structure and putative function of small Toprim domain-containing protein from Bacillus stearothermophilusStructural basis for gate-DNA recognition and bending by type IIA topoisomerasesCrystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigationA novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerasesThe archaeo-eukaryotic primase of plasmid pRN1 requires a helix bundle domain for faithful primer synthesisStructural Insights into the Quinolone Resistance Mechanism of Mycobacterium tuberculosis DNA GyraseBinding Mechanism of Metal⋅NTP Substrates and Stringent-Response Alarmones to Bacterial DnaG-Type PrimasesStructure of a topoisomerase II–DNA–nucleotide complex reveals a new control mechanism for ATPase activityStructural and mechanistic insight into Holliday-junction dissolution by Topoisomerase IIIα and RMI1Identification of residues in yeast Spo11p critical for meiotic DNA double-strand break formation.A proposal: Evolution of PCNA's role as a marker of newly replicated DNAPhylogenomics of type II DNA topoisomerasesAtSPO11-1 is necessary for efficient meiotic recombination in plants.RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms.Manual classification strategies in the ECOD database.Metal ion and inter-domain interactions as functional networks in E. coli topoisomerase I.Recovery of the poisoned topoisomerase II for DNA religation: coordinated motion of the cleavage core revealed with the microsecond atomistic simulation.Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA.On the origin of the translation system and the genetic code in the RNA world by means of natural selection, exaptation, and subfunctionalization.The RAGNYA fold: a novel fold with multiple topological variants found in functionally diverse nucleic acid, nucleotide and peptide-binding proteinsMutL homologs in restriction-modification systems and the origin of eukaryotic MORC ATPases.The ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks.A new family of polymerases related to superfamily A DNA polymerases and T7-like DNA-dependent RNA polymerases.Hidden chromosome symmetry: in silico transformation reveals symmetry in 2D DNA walk trajectories of 671 chromosomes.The DNA relaxation activity and covalent complex accumulation of Mycobacterium tuberculosis topoisomerase I can be assayed in Escherichia coli: application for identification of potential FRET-dye labeling sites.
P2860
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P2860
Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins.
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@ast
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@en
type
label
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@ast
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@en
prefLabel
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@ast
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@en
P2860
P356
P1476
Toprim--a conserved catalytic ...... y nucleases and RecR proteins.
@en
P2093
P2860
P304
P356
10.1093/NAR/26.18.4205
P407
P577
1998-09-01T00:00:00Z