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Identification of Bacterial Protein Interaction Partners Points to New Intracellular Functions ofFrancisella tularensisGlyceraldehyde-3-Phosphate Dehydrogenase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F20%3A00556241" target="_blank" >RIV/60162694:G44__/20:00556241 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.frontiersin.org/journals/microbiology#" target="_blank" >https://www.frontiersin.org/journals/microbiology#</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3389/fmicb.2020.576618" target="_blank" >10.3389/fmicb.2020.576618</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Identification of Bacterial Protein Interaction Partners Points to New Intracellular Functions ofFrancisella tularensisGlyceraldehyde-3-Phosphate Dehydrogenase

  • Original language description

    Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is well known for its involvement in numerous non-metabolic processes inside mammalian cells. Alternative functions of prokaryotic GAPDH are mainly deduced from its extracellular localization ability to bind to selected host proteins. Data on its participation in intracellular bacterial processes are scarce as there has been to date only one study dealing with this issue. We previously have reported several points of evidence that the GAPDH homolog ofFrancisella tularensisGapA might also exert additional non-enzymatic functions. Following on from our earlier observations we decided to identify GapA's interacting partners within the bacterial proteome to explore its new roles at intracellular level. The quantitative proteomics approach based on stable isotope labeling of amino acids in cell culture (SILAC) in combination with affinity purification mass spectrometry enabled us to identify 18 proteins potentially interacting with GapA. Six of those interactions were further confirmed by alternative methods. Half of the identified proteins were involved in non-metabolic processes. Further analysis together with quantitative label-free comparative analysis of proteomes isolated from the wild-type strain strain with deletedgapAgene suggests that GapA is implicated in DNA repair processes. Absence of GapA promotes secretion of its most potent interaction partner the hypothetical protein with peptidase propeptide domain (PepSY) thereby indicating that it impacts on subcellular distribution of some proteins.

  • 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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Frontiers in Microbiology

  • ISSN

    1664-302X

  • e-ISSN

    1664-302X

  • Volume of the periodical

    11

  • Issue of the periodical within the volume

    September

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    14

  • Pages from-to

    576618

  • UT code for WoS article

    000575378800001

  • EID of the result in the Scopus database

    2-s2.0-85091489884