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Active site alanine mutations convert deubiquitinases into high-affinity ubiquitinbinding proteins

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17110%2F18%3AA1901Z5C" target="_blank" >RIV/61988987:17110/18:A1901Z5C - isvavai.cz</a>

  • Result on the web

    <a href="https://apps.webofknowledge.com/full_record.do?product=WOS&search_mode=GeneralSearch&qid=39&SID=C2ThWyDX6vtBzFEKIZA&page=1&doc=1" target="_blank" >https://apps.webofknowledge.com/full_record.do?product=WOS&search_mode=GeneralSearch&qid=39&SID=C2ThWyDX6vtBzFEKIZA&page=1&doc=1</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.15252/embr.201745680" target="_blank" >10.15252/embr.201745680</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Active site alanine mutations convert deubiquitinases into high-affinity ubiquitinbinding proteins

  • Original language description

    A common strategy for exploring the biological roles of deubiquitinating enzymes (DUBs) in different pathways is to study the effects of replacing the wild-type DUB with a catalytically inactive mutant in cells. We report here that a commonly studied DUB mutation, in which the catalytic cysteine is replaced with alanine, can dramatically increase the affinity of some DUBs for ubiquitin. Overexpression of these tight-binding mutants thus has the potential to sequester cellular pools of monoubiquitin and ubiquitin chains. As a result, cells expressing these mutants may display unpredictable dominant negative physiological effects that are not related to loss of DUB activity. The structure of the SAGA DUB module bound to free ubiquitin reveals the structural basis for the 30-fold higher affinity of Ubp8(C146A) for ubiquitin. We show that an alternative option, substituting the active site cysteine with arginine, can inactivate DUBs while also decreasing the affinity for ubiquitin.

  • 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

    30204 - Oncology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    EMBO REP

  • ISSN

    1469-221X

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

  • UT code for WoS article

    000446430400008

  • EID of the result in the Scopus database

    2-s2.0-85052479055