The helical domain of the EcoR1241 motor subunit participates in ATPase activity and dsDNA translocation

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00473698" target="_blank" >RIV/61388971:_____/17:00473698 - isvavai.cz</a>

Alternative codes found

RIV/60076658:12310/17:43895562

Result on the web

<a href="http://dx.doi.org/10.7717/peerj.2887" target="_blank" >http://dx.doi.org/10.7717/peerj.2887</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.7717/peerj.2887" target="_blank" >10.7717/peerj.2887</a>

Result language

angličtina

Original language name

The helical domain of the EcoR1241 motor subunit participates in ATPase activity and dsDNA translocation

Original language description

Type I restriction-modification enzymes are multisubunit, multifunctional molecular machines that recognize specific DNA target sequences, and their multisubunit organization underlies their multifunctionality. EcoR124I is the archetype of Type I restriction-modification family IC and is composed of three subunit types: HsdS, HsdM, and HsdR. DNA cleavage and ATP-dependent DNA translocation activities are housed in the distinct domains of the endonuclease/motor subunit HsdR. Because the multiple functions are integrated in this large subunit of 1,038 residues, a large number of interdomain contacts might be expected. The crystal structure of EcoR124I HsdR reveals a surprisingly sparse number of contacts between helicase domain 2 and the C-terminal helical domain that is thought to be involved in assembly with HsdM. Only two potential hydrogen-bonding contacts are found in a very small contact region. In the present work, the relevance of these two potential hydrogen-bonding interactions for the multiple activities of EcoR124I is evaluated by analysing mutant enzymes using in vivo and in vitro experiments. Molecular dynamics simulations are employed to provide structural interpretation of the functional data. The results indicate that the helical domain is involved in the DNA translocation, cleavage, and ATPase activities of HsdR, and a role in controlling those activities is suggested.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

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

Name of the periodical

PeerJ

ISSN

2167-8359

e-ISSN

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Volume of the periodical

5

Issue of the periodical within the volume

JAN 18

Country of publishing house

US - UNITED STATES

Number of pages

23

Pages from-to

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UT code for WoS article

000394700600006

EID of the result in the Scopus database

2-s2.0-85013187990