All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Cofactor induced dissociation of the multifunctional multisubunit EcoR124I investigated using electromobility shift assays, AFM and SPR

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00477805" target="_blank" >RIV/61388971:_____/17:00477805 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1039/c7ra07505g" target="_blank" >http://dx.doi.org/10.1039/c7ra07505g</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/c7ra07505g" target="_blank" >10.1039/c7ra07505g</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Cofactor induced dissociation of the multifunctional multisubunit EcoR124I investigated using electromobility shift assays, AFM and SPR

  • Original language description

    We have applied three techniques to the study of subunit assembly of the Type IC Restriction-Modification enzyme EcoR124I. This fully functional enzyme EcoR124I consists of a complex of the three subunits HsdR, HsdM and HsdS in a R2M2S1 stoichiometry, but is known to dissociate readily, releasing free HsdR and producing first an R-1-complex and then the core, DNA-binding methyltransferase (M2S1) complex. Analysis of the assembly pathway of this enzyme has previously employed gel retardation and Surface Plasmon Resonance (SPR), but the studies to date have not included the cofactors required for full enzyme activity. In this paper, we have also used atomic force microscopy (AFM)-based molecular volume measurements, and have analysed the effect of the cofactors ATP and AdoMet on enzyme stability and subunit assembly. We compare the data obtained from all three techniques and we show that they all give consistent results, but inherent differences in the methodologies provide additional information useful for the study of subunit assembly.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • 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

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

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    RSC Advances

  • ISSN

    2046-2069

  • e-ISSN

  • Volume of the periodical

    7

  • Issue of the periodical within the volume

    61

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

    38737-38746

  • UT code for WoS article

    000407442000072

  • EID of the result in the Scopus database

    2-s2.0-85027237337