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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

  • 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

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • 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