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Monitoring RAYT activity by surface plasmon resonance biosensor

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985882%3A_____%2F15%3A00452057" target="_blank" >RIV/67985882:_____/15:00452057 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/15:00452057

  • Result on the web

    <a href="http://dx.doi.org/10.1007/s00216-015-8491-y" target="_blank" >http://dx.doi.org/10.1007/s00216-015-8491-y</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00216-015-8491-y" target="_blank" >10.1007/s00216-015-8491-y</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Monitoring RAYT activity by surface plasmon resonance biosensor

  • Original language description

    The process of DNA transposition involves the binding, cleavage, and recombination of specific DNA segments (transposable elements, TE) and is catalyzed by special enzymes encoded by the TE transposases. REP-associated tyrosine transposases (RAYTs) are aclass of Y1 nucleases related to the IS200/IS605 transposases associated with a bacterial TE known as repetitive extragenic palindrome elements (REPs). Although RAYT has been subject of numerous studies, where DNA binding and cleavage by RAYT have beenconfirmed for Escherichia coli, the molecular mechanism of DNA insertion has not been fully understood. In this work, it is demonstrated that surface plasmon resonance (SPR) biosensor technology combined with a system of DNA hairpin probes (mimicking thenatural REP sequence) and short oligonucleotides (ONs) can provide a rapid and real-time platform for monitoring and quantification of RAYT activity. We utilized RAYT from E. coli (strain MG1655) as a model system, where we evaluated its

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    JA - Electronics and optoelectronics

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP305%2F12%2F1801" target="_blank" >GAP305/12/1801: Molecular mechanisms of association of a novel type of transposase with repetitive palindromic elements</a><br>

  • 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

    Analytical and Bioanalytical Chemistry

  • ISSN

    1618-2642

  • e-ISSN

  • Volume of the periodical

    407

  • Issue of the periodical within the volume

    14

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    9

  • Pages from-to

    3985-3993

  • UT code for WoS article

    000354190300009

  • EID of the result in the Scopus database

    2-s2.0-84939548760