Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00533326" target="_blank" >RIV/61388971:_____/20:00533326 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/20:10413059
Result on the web
<a href="http://dx.doi.org/10.1074/jbc.RA120.014122" target="_blank" >http://dx.doi.org/10.1074/jbc.RA120.014122</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.RA120.014122" target="_blank" >10.1074/jbc.RA120.014122</a>
Alternative languages
Result language
angličtina
Original language name
Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins
Original language description
In a wide range of organisms, from bacteria to humans, numerous proteins have to be posttranslationally acylated to become biologically active. Bacterialrepeats intoxin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo posttranslational acylation on ?-amino groups of two internal conserved lysine residues by co-expressed toxin-activating acyltransferases. Here, we investigated how the chemical nature, position, and number of bound acyl chains govern the activities ofBordetella pertussisadenylate cyclase toxin (CyaA),Escherichia coli?-hemolysin (HlyA), andKingella kingaecytotoxin (RtxA). We found that the three protoxins are acylated in the sameE. colicell background by each of the CyaC, HlyC, and RtxC acyltransferases. We also noted that the acyltransferase selects from the bacterial pool of acyl?acyl carrier proteins (ACPs) an acyl chain of a specific length for covalent linkage to the protoxin. The acyltransferase also selects whether both or only one of two conserved lysine residues of the protoxin will be posttranslationally acylated. Functional assays revealed that RtxA has to be modified by 14-carbon fatty acyl chains to be biologically active, that HlyA remains active also when modified by 16-carbon acyl chains, and that CyaA is activated exclusively by 16-carbon acyl chains. These results suggest that the RTX toxin molecules are structurally adapted to the length of the acyl chains used for modification of their acylated lysine residue in the second, more conserved acylation site.
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
—
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 Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
295
Issue of the periodical within the volume
28
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
9268-9280
UT code for WoS article
000552758600001
EID of the result in the Scopus database
2-s2.0-85088202515