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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

Frontiers in Microbiology

ISSN

1664-302X

e-ISSN

1664-302X

Svazek periodika

11

Číslo periodika v rámci svazku

September

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

14

Strana od-do

576618

Kód UT WoS článku

000575378800001

EID výsledku v databázi Scopus

2-s2.0-85091489884