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

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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

Czech name

Vztah helikasové a nukleasové domény během translokace DNA molekulárním motorem EcoR124I

Czech 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 fyzikálněvázanými 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

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

<a href="/en/project/GA204%2F07%2F0325" target="_blank" >GA204/07/0325: Identification of amino acid residues of the HsdS and HsdR subunits required for correct assembly of Type I restriction-modification enzyme EcoR124I</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2008

Confidentiality

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

Name of the periodical

Journal of Molecular Biology

ISSN

0022-2836

e-ISSN

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Volume of the periodical

384

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

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UT code for WoS article

000262016600021

EID of the result in the Scopus database

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