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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
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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