Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43887443" target="_blank" >RIV/60076658:12310/14:43887443 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/14:00437252 RIV/61388971:_____/14:00437252

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs00894-014-2334-1" target="_blank" >http://link.springer.com/article/10.1007%2Fs00894-014-2334-1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-014-2334-1" target="_blank" >10.1007/s00894-014-2334-1</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I

Popis výsledku v původním jazyce

Restriction-modification systems protect bacteria from foreign DNA. Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA-cleavage and ATP-dependent DNA translocation activities located on endonuclease/motor subunit HsdR. The recent structure of the first intact motor subunit of the type I restriction enzyme from plasmid EcoR124I suggested a mechanism by which stalled translocation triggers DNA cleavage via a lysine residue on the endonuclease domain that contacts ATP bound between the two helicase domains. In the present work, molecular dynamics simulations are used to explore this proposal. Molecular dynamics simulations suggest that the Lys-ATP contact alternates with a contact with a nearby loop housing the conserved QxxxY motif that had been implicated in DNA cleavage. This model is tested here using in vivo and in vitro experiments. The results indicate how local interactions are transduced to domain motions within the endonuclease/motor subun

Název v anglickém jazyce

Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I

Popis výsledku anglicky

Restriction-modification systems protect bacteria from foreign DNA. Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA-cleavage and ATP-dependent DNA translocation activities located on endonuclease/motor subunit HsdR. The recent structure of the first intact motor subunit of the type I restriction enzyme from plasmid EcoR124I suggested a mechanism by which stalled translocation triggers DNA cleavage via a lysine residue on the endonuclease domain that contacts ATP bound between the two helicase domains. In the present work, molecular dynamics simulations are used to explore this proposal. Molecular dynamics simulations suggest that the Lys-ATP contact alternates with a contact with a nearby loop housing the conserved QxxxY motif that had been implicated in DNA cleavage. This model is tested here using in vivo and in vitro experiments. The results indicate how local interactions are transduced to domain motions within the endonuclease/motor subun

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GAP207%2F12%2F2323" target="_blank" >GAP207/12/2323: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

—

Svazek periodika

20

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

000339884800015

EID výsledku v databázi Scopus

—