The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.)

Research output: Contribution to journalArticle

Abstract

The biosynthesis of chlorophyll has been demonstrated to require an extensive set of enzymes, the initial stages of which are shared with the synthesis of heme. Of these enzymes, the most enigmatic is the Mg-protoporphyrin IX monomethyl ester cyclase (EC 1.14.13.81). This enzyme requires components found associated with the plastid membrane and the plastid soluble fraction. One of the components, XanL, is found associated with the membrane and another protein, Ycf54, has recently been identified based upon association with XanL. This study describes a deeper analysis of the role of Ycf54 in the enzyme and the localization of the protein in barley plastids. The results clearly demonstrate a strong association of Ycf54 with XanL, absence of Ycf54 from soluble fractions necessary for activity and more evidence for a third membrane localized component of the enzyme.

Details

Authors
External organisations
  • Carlsberg Research Center / Carlsberg Laboratory
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology

Keywords

  • Mg-protoporphyrin monomethyl ester, Protoporphyrins/metabolism, Plastids/metabolism, Plant Proteins/chemistry/genetics/*metabolism, Oxygenases/chemistry/genetics/*metabolism, Mutation, Plant, Genes, Hordeum/genetics/*metabolism, chlorophyll, cyclase, etioplast, isocyclic ring
Original languageEnglish
Pages (from-to)2377-2386
JournalThe FEBS Journal
Volume281
Issue number10
Publication statusPublished - 2014
Publication categoryResearch
Peer-reviewedYes
Externally publishedYes

Bibliographic note

10