Functional Coupling of Duplex Translocation to DNA Cleavage in a Type I Restriction Enzyme
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F15%3A00452784" target="_blank" >RIV/68378050:_____/15:00452784 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00452784 RIV/67179843:_____/15:00452784 RIV/60076658:12310/15:43888966
Result on the web
<a href="http://dx.doi.org/10.1371/journal.pone.0128700" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0128700</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0128700" target="_blank" >10.1371/journal.pone.0128700</a>
Alternative languages
Result language
angličtina
Original language name
Functional Coupling of Duplex Translocation to DNA Cleavage in a Type I Restriction Enzyme
Original language description
Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on motor subunit HsdR. Functional coupling of DNA cleavage and translocation is a hallmark of the Type I restriction systems that is consistent with their proposed role in horizontal gene transfer. DNA cleavage occurs at nonspecific sites distant from the cognate recognition sequence, apparently triggered by stalled translocation. The X-ray crystal structure of the complete HsdR subunit from E. coli plasmid R124 suggested that the triggering mechanism involves interdomain contacts mediated by ATP. In the present work, in vivo and in vitro activity assays and crystal structures of three mutants of EcoR124I HsdR designed to probe this mechanism are reported. The results indicate that interdomain engagement via ATP is indeed responsible for signal transmission between the endonuclease and helicase domains of the motor subunit. A previously identified sequence motif that is shared by the RecB nucleases and some Type I endonucleases is implicated in signaling.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
PLoS ONE
ISSN
1932-6203
e-ISSN
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Volume of the periodical
10
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
21
Pages from-to
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UT code for WoS article
000355700700118
EID of the result in the Scopus database
2-s2.0-84934974264