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The role of fatty acylation in activity of proteins
Grobarčíková, Michaela ; Mašín, Jiří (advisor) ; Petráčková, Denisa (referee)
Post-translational modifications are covalent and generally enzyme-mediated modifications of proteins. These modifications can serve to create active forms of proteins and they can also expand the cellular repertoire of proteins derived from standard amino acids. Known post-translational modifications include for example phosphorylation, glycosylation, ubiquitination, proteolysis and also acylation discussed in more detail in this thesis. Acylation of proteins, the covalent attachment of an acyl group, is a very frequent protein modification. This reaction is typically mediated by specific acyl transferases and involves transport of an acyl group from a donor to an amino acid residue. A diverse spectrum of cellular proteins is post-translationally acylated and therefore become biologically active. This phenomenon occurs in bacterial toxins, which are important factors of the virulence of pathogenic bacteria. Protein lipidation regulates numerous biological pathways such as membrane targeting, protein secretion, cell signaling, and apoptosis. Posttranslational acylation is also required for Ras activity and many other cancer-causing proteins. Therefore, inhibitors of acyltransferases of these proteins are being tested as targets for antitumor drugs. In this work, findings about individual types of...
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