Vztah helikasové a nukleasové domény během translokace DNA molekulárním motorem EcoR124I

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F08%3A00317626" target="_blank" >RIV/61388971:_____/08:00317626 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The Interrelationship of Helicase and Nuclease Domains during DNA Translocation by the Molecular Motor EcoR124I

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

The Interrelationship of Helicase and Nuclease Domains during DNA Translocation by the Molecular Motor EcoR124I

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/GA204%2F07%2F0325" target="_blank" >GA204/07/0325: Identifikace aminokyselinových zbytků podjednotek HsdS a HsdR nutných pro správné sestavení restrikčně-modifikačního enzymu Typu I EcoR124I</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Biology

ISSN

0022-2836

e-ISSN

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Svazek periodika

384

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

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Kód UT WoS článku

000262016600021

EID výsledku v databázi Scopus

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