The Cys4 zinc finger of bacteriophage T7 primase in sequence-specific single-stranded DNA recognition.
about
Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new membersStructure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcriptionStructure and function of primase RepB' encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand modeTwo distantly homologous DnaG primases from Thermoanaerobacter tengcongensis exhibit distinct initiation specificities and priming activitiesInteraction of ribonucleoside triphosphates with the gene 4 primase of bacteriophage T7.Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex.DNA recognition by the DNA primase of bacteriophage T7: a structure-function study of the zinc-binding domain.Direct role for the RNA polymerase domain of T7 primase in primer delivery.Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactionsMechanism of sequence-specific template binding by the DNA primase of bacteriophage T7The N-terminal domain of the Drosophila mitochondrial replicative DNA helicase contains an iron-sulfur cluster and binds DNAZinc-binding domain of the bacteriophage T7 DNA primase modulates binding to the DNA template.The Arabidopsis At1g30680 gene encodes a homologue to the phage T7 gp4 protein that has both DNA primase and DNA helicase activities.Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Interactions of the vaccinia virus A19 proteinA mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently.The roles of tryptophans in primer synthesis by the DNA primase of bacteriophage T7.Complete Genome Sequence of Citrobacter freundii Myophage Merlin.DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: implications for active site communication.Understanding helicases as a means of virus control.Discrete interactions between bacteriophage T7 primase-helicase and DNA polymerase drive the formation of a priming complex containing two copies of DNA polymerase.Hyperthermophilic topoisomerase I from Thermotoga maritima. A very efficient enzyme that functions independently of zinc binding.Primer initiation and extension by T7 DNA primaseInteraction of bacteriophage T7 gene 4 primase with its template recognition site.Acidic residues in the nucleotide-binding site of the bacteriophage T7 DNA primase.A molecular handoff between bacteriophage T7 DNA primase and T7 DNA polymerase initiates DNA synthesis.Class-specific restrictions define primase interactions with DNA template and replicative helicase.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.The N-terminal domain of TWINKLE contributes to single-stranded DNA binding and DNA helicase activities.Essential lysine residues in the RNA polymerase domain of the gene 4 primase-helicase of bacteriophage T7.Plant organellar DNA primase-helicase synthesizes RNA primers for organellar DNA polymerases using a unique recognition sequence.Chimeric proteins constructed from bacteriophage T7 gp4 and a putative primase-helicase from Arabidopsis thaliana.
P2860
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P2860
The Cys4 zinc finger of bacteriophage T7 primase in sequence-specific single-stranded DNA recognition.
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The Cys4 zinc finger of bacter ...... ngle-stranded DNA recognition.
@ast
The Cys4 zinc finger of bacter ...... ngle-stranded DNA recognition.
@en
type
label
The Cys4 zinc finger of bacter ...... ngle-stranded DNA recognition.
@ast
The Cys4 zinc finger of bacter ...... ngle-stranded DNA recognition.
@en
prefLabel
The Cys4 zinc finger of bacter ...... ngle-stranded DNA recognition.
@ast
The Cys4 zinc finger of bacter ...... ngle-stranded DNA recognition.
@en
P2093
P2860
P356
P1476
The Cys4 zinc finger of bacter ...... ingle-stranded DNA recognition
@en
P2093
C C Richardson
S G Hyberts
T Kusakabe
P2860
P304
P356
10.1073/PNAS.96.8.4295
P407
P50
P577
1999-04-01T00:00:00Z