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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F08%3A00317626%21RIV09-AV0-61388971
rdf:type
skos:Concept n15:Vysledek
dcterms:description
Restrikčně – modifikační enzym Typu I EcoR124I je složen ze tří podjednotek v poměru HsdR2:HsdM2:HsdS1. Podjednotka HsdR je příkladem archetypu fuse mezi nukleasovou a helikasovou doménou do jednoho polypeptidu. Zkoumali jsme vztah mezi těmito fyzikálně vázanými doménami analýzou DNA translokačních vlastností komplexu EcoR124I, kde HsdR podjednotky nesly mutace v RecB-nucleasovém motivu II nebo III. Mutace v nukleasové doméně ovlivňují translokaci DNA přestože jsou od helikasové domény odděleny. Kromě redukce restrikční aktivity jsme také pozorovali sníženou rychlost translokace a ATPasové aktivity; rozdílné populace enzymů s rozdílnými charakteristikami translokační rychlosti; tendenci k zastavování během iniciace translokace; a změněnou dynamiku turnoveru HsdR The Type I Restriction-Modification enzyme EcoR124I comprises three subunits with the stoichiometry HsdR2:HsdM2:HsdS1. The HsdR subunits are archetypical examples of the fusion between nuclease and helicase domains into a single polypeptide, a linkage that is found in a great many other DNA processing enzymes. To explore the interrelationship between these physically-linked domains, we examined the DNA translocation properties of EcoR124I complexes in which the HsdR subunits had been mutated in the RecB-like nuclease motifs II or III. We found that nuclease mutations could have noteworthy effects on DNA translocation despite being discrete from the helicase domain. In addition to reductions in DNA cleavage activity, we also observed: decreased translocation and ATPase rates; different enzyme populations with different characteristic translocation rates; a tendency to stall during initiation; and, altered HsdR turnover dynamics The Type I Restriction-Modification enzyme EcoR124I comprises three subunits with the stoichiometry HsdR2:HsdM2:HsdS1. The HsdR subunits are archetypical examples of the fusion between nuclease and helicase domains into a single polypeptide, a linkage that is found in a great many other DNA processing enzymes. To explore the interrelationship between these physically-linked domains, we examined the DNA translocation properties of EcoR124I complexes in which the HsdR subunits had been mutated in the RecB-like nuclease motifs II or III. We found that nuclease mutations could have noteworthy effects on DNA translocation despite being discrete from the helicase domain. In addition to reductions in DNA cleavage activity, we also observed: decreased translocation and ATPase rates; different enzyme populations with different characteristic translocation rates; a tendency to stall during initiation; and, altered HsdR turnover dynamics
dcterms:title
The Interrelationship of Helicase and Nuclease Domains during DNA Translocation by the Molecular Motor EcoR124I The Interrelationship of Helicase and Nuclease Domains during DNA Translocation by the Molecular Motor EcoR124I Vztah helikasové a nukleasové domény během translokace DNA molekulárním motorem EcoR124I
skos:prefLabel
Vztah helikasové a nukleasové domény během translokace DNA molekulárním motorem EcoR124I The Interrelationship of Helicase and Nuclease Domains during DNA Translocation by the Molecular Motor EcoR124I The Interrelationship of Helicase and Nuclease Domains during DNA Translocation by the Molecular Motor EcoR124I
skos:notation
RIV/61388971:_____/08:00317626!RIV09-AV0-61388971
n3:aktivita
n13:Z n13:P
n3:aktivity
P(GA204/07/0325), Z(AV0Z50200510)
n3:cisloPeriodika
5
n3:dodaniDat
n5:2009
n3:domaciTvurceVysledku
n14:9647864 n14:1646869
n3:druhVysledku
n4:J
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n12:predkladatel
n3:idSjednocenehoVysledku
373033
n3:idVysledku
RIV/61388971:_____/08:00317626
n3:jazykVysledku
n18:eng
n3:klicovaSlova
single molecule; enzyme disorder; translocase
n3:klicoveSlovo
n16:translocase n16:enzyme%20disorder n16:single%20molecule
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[ECCF815734AF]
n3:nazevZdroje
Journal of Molecular Biology
n3:obor
n11:EE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
5
n3:projekt
n7:GA204%2F07%2F0325
n3:rokUplatneniVysledku
n5:2008
n3:svazekPeriodika
384
n3:tvurceVysledku
Weiserová, Marie Šišáková, Eva Szczelkun, M. D. Dekker, C. Seidel, R.
n3:wos
000262016600021
n3:zamer
n17:AV0Z50200510
s:issn
0022-2836
s:numberOfPages
14