Bordetella pertussis Acetylome is Shaped by Lysine Deacetylase Bkd1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00533031" target="_blank" >RIV/61388971:_____/20:00533031 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/abs/10.1021/acs.jproteome.0c00178" target="_blank" >https://pubs.acs.org/doi/abs/10.1021/acs.jproteome.0c00178</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jproteome.0c00178" target="_blank" >10.1021/acs.jproteome.0c00178</a>
Alternative languages
Result language
angličtina
Original language name
Bordetella pertussis Acetylome is Shaped by Lysine Deacetylase Bkd1
Original language description
Post-translational modifications of proteins enable swift physiological adaptation of cells to altered growth conditions and stress. Aside from protein phosphorylation, acetylation on epsilon-amino groups of lysine residues (N-epsilon-lysine acetylation) represents another important post-translational modification of proteins. For many bacterial pathogens, including the whooping cough agent Bordetella pertussis, the role and extent of protein acetylation remain to be defined. We expressed in Escherichia coli the BP0960 and BP3063 genes encoding two putative deacetylases of B. pertussis and show that BP0960 encodes a lysine deacetylase enzyme, named Bkd1, that regulates acetylation of a range of B. pertussis proteins. Comparison of the proteome and acetylome of a Delta bkd1 mutant with the proteome and acetylome of wild-type B. pertussis (PRIDE ID. PXD016384) revealed that acetylation on lysine residues may modulate activities or stabilities of proteins involved in bacterial metabolism and histone-like proteins. However, increased acetylation of the BvgA response regulator protein of the B. pertussis master virulence-regulating BvgAS two-component system affected neither the total levels of produced BvgA nor its phosphorylation status. Indeed, the Delta bkd1 mutant was not impaired in the production of key virulence factors and its survival within human macrophages in vitro was not affected. The Delta bkd1 mutant exhibited an increased growth rate under carbon source-limiting conditions and its virulence in the in vivo mouse lung infection model was somewhat affected. These results indicate that the lysine deacetylase Bkd1 and N-epsilon-lysine acetylation primarily modulate the general metabolism rather than the virulence of B. pertussis.
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
Result was created during the realization of more than one project. More information in the Projects tab.
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
Journal of Proteome Research
ISSN
1535-3893
e-ISSN
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Volume of the periodical
19
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
17
Pages from-to
3680-3696
UT code for WoS article
000569378700009
EID of the result in the Scopus database
2-s2.0-85090491168