A β-hairpin epitope as novel structural requirement for protein arginine rhamnosylation†
| Autor: | Marthe T. C. Walvoort, Ioli Kotsogianni, Nathaniel I. Martin, Liubov Yakovlieva, Johan Kemmink, Franziska Koller, Thomas M. Wood, Juergen Lassak |
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| Přispěvatelé: | Chemical Biology 2, Stratingh Institute of Chemistry |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Glycosylation Arginine Peptide General Chemistry 010402 general chemistry 01 natural sciences Epitope Cyclic peptide 0104 chemical sciences 03 medical and health sciences Residue (chemistry) chemistry.chemical_compound Chemistry chemistry Biochemistry Recognition sequence Asparagine Peptide sequence 030304 developmental biology |
| Zdroj: | Chemical Science Chemical Science, 12(4), 1560-1567 Chemical Science, 12(4), 1560-1567. ROYAL SOC CHEMISTRY |
| ISSN: | 2041-6539 2041-6520 |
| Popis: | For canonical asparagine glycosylation, the primary amino acid sequence that directs glycosylation at specific asparagine residues is well-established. Here we reveal that a recently discovered bacterial enzyme EarP, that transfers rhamnose to a specific arginine residue in its acceptor protein EF-P, specifically recognizes a β-hairpin loop. Notably, while the in vitro rhamnosyltransferase activity of EarP is abolished when presented with linear substrate peptide sequences derived from EF-P, the enzyme readily glycosylates the same sequence in a cyclized β-hairpin mimic. Additional studies with other substrate-mimicking cyclic peptides revealed that EarP activity is sensitive to the method used to induce cyclization and in some cases is tolerant to amino acid sequence variation. Using detailed NMR approaches, we established that the active peptide substrates all share some degree of β-hairpin formation, and therefore conclude that the β-hairpin epitope is the major determinant of arginine-rhamnosylation by EarP. Our findings add a novel recognition motif to the existing knowledge on substrate specificity of protein glycosylation, and are expected to guide future identifications of rhamnosylation sites in other protein substrates. For bacterial arginine rhamnosylation, the rhamnosyltransferase EarP specifically recognizes a β-hairpin structure in the acceptor substrate. |
| Databáze: | OpenAIRE |
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