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Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00431504" target="_blank" >RIV/61388963:_____/14:00431504 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1002/pro.2497" target="_blank" >http://dx.doi.org/10.1002/pro.2497</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/pro.2497" target="_blank" >10.1002/pro.2497</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations

  • Original language description

    The nuclease domain of colicin E7 (NColE7) promotes the nonspecific cleavage of nucleic acids at its C-terminal HNH motif. Interestingly, the deletion of four N-terminal residues (446-449 NColE7=KRNK) resulted in complete loss of the enzyme activity. R447A mutation was reported to decrease the nuclease activity, but a detailed analysis of the role of the highly positive and flexible N-terminus is still missing. Here, we present the study of four mutants, with a decreased activity in the following order:NColE7 > KGNK > KGNG similar to GGNK > GGNG. At the same time, the folding, the metal-ion, and the DNA-binding affinity were unaffected by the mutations as revealed by linear and circular dichroism spectroscopy, isothermal calorimetric titrations, and gel mobility shift experiments. Semiempirical quantum chemical calculations and molecular dynamics simulations revealed that K446, K449, and/or the N-terminal amino group are able to approach the active centre in the absence of the other p

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2014

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Protein Science

  • ISSN

    0961-8368

  • e-ISSN

  • Volume of the periodical

    23

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    1113-1122

  • UT code for WoS article

    000339664800010

  • EID of the result in the Scopus database