Show simple item record

dc.contributor.authorSternicki, Louise M
dc.contributor.authorNguyen, Stephanie
dc.contributor.authorPacholarz, Kamila J
dc.contributor.authorBarran, Perdita
dc.contributor.authorPendini, Nicole R
dc.contributor.authorBooker, Grant W
dc.contributor.authorHuet, Yoann
dc.contributor.authorBaltz, Rachel
dc.contributor.authorWegener, Kate L
dc.contributor.authorPukala, Tara L
dc.contributor.authorPolyak, Steven W
dc.date.accessioned2021-04-22T03:59:05Z
dc.date.available2021-04-22T03:59:05Z
dc.date.issued2020
dc.identifier.issn0003-9861
dc.identifier.doi10.1016/j.abb.2020.108509
dc.identifier.urihttp://hdl.handle.net/10072/403891
dc.description.abstractBiotin protein ligase (BPL) is an essential enzyme in all kingdoms of life, making it a potential target for novel anti-infective agents. Whilst bacteria and archaea have simple BPL structures (class I and II), the homologues from certain eukaryotes such as mammals, insects and yeast (class III) have evolved a more complex structure with a large extension on the N-terminus of the protein in addition to the conserved catalytic domain. The absence of atomic resolution structures of any class III BPL hinders structural and functional analysis of these enzymes. Here, two new class III BPLs from agriculturally important moulds Botrytis cinerea and Zymoseptoria tritici were characterised alongside the homologue from the prototypical yeast Saccharomyces cerevisiae. Circular dichroism and ion mobility-mass spectrometry analysis revealed conservation of the overall tertiary and secondary structures of all three BPLs, corresponding with the high sequence similarity. Subtle structural differences were implied by the different thermal stabilities of the enzymes and their varied Michaelis constants for their interactions with ligands biotin, MgATP, and biotin-accepting substrates from different species. The three BPLs displayed different preferences for fungal versus bacterial protein substrates, providing further evidence that class III BPLs have a ‘substrate validation’ activity for selecting only appropriate proteins for biotinylation. Selective, potent inhibition of these three BPLs was demonstrated despite sequence and structural homology. This highlights the potential for targeting BPL for novel, selective antifungal therapies against B. cinerea, Z. tritici and other fungal species.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherElsevier
dc.relation.ispartofjournalArchives of Biochemistry and Biophysics
dc.relation.ispartofvolume691
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchcode3101
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsBiochemistry & Molecular Biology
dc.subject.keywordsBiophysics
dc.subject.keywordsBiotin
dc.titleBiochemical characterisation of class III biotin protein ligases from Botrytis cinerea and Zymoseptoria tritici
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationSternicki, LM; Nguyen, S; Pacholarz, KJ; Barran, P; Pendini, NR; Booker, GW; Huet, Y; Baltz, R; Wegener, KL; Pukala, TL; Polyak, SW, Biochemical characterisation of class III biotin protein ligases from Botrytis cinerea and Zymoseptoria tritici, Archives of Biochemistry and Biophysics, 2020, 691
dcterms.dateAccepted2020-07-16
dc.date.updated2021-04-22T02:59:02Z
gro.hasfulltextNo Full Text
gro.griffith.authorSternicki, Louise


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record