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

Bollivar, D.; Braumann, I.; Berendt, K.; Gough, S. P. and Hansson, Mats LU (2014) In The FEBS Journal 281(10). p.2377-2386
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... (More)
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. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
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
in
The FEBS Journal
volume
281
issue
10
pages
2377 - 2386
publisher
Federation of European Neuroscience Societies and Blackwell Publishing Ltd
external identifiers
  • scopus:84901233802
ISSN
1742-464X
DOI
10.1111/febs.12790
language
English
LU publication?
no
id
7f2cebc2-d4d7-4871-8560-0aa1614ad6f9 (old id 8001695)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/24661504
date added to LUP
2015-09-30 09:32:58
date last changed
2017-07-02 03:04:00
@article{7f2cebc2-d4d7-4871-8560-0aa1614ad6f9,
  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.},
  author       = {Bollivar, D. and Braumann, I. and Berendt, K. and Gough, S. P. and Hansson, Mats},
  issn         = {1742-464X},
  keyword      = {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},
  language     = {eng},
  number       = {10},
  pages        = {2377--2386},
  publisher    = {Federation of European Neuroscience Societies and Blackwell Publishing Ltd},
  series       = {The FEBS Journal},
  title        = {The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.)},
  url          = {http://dx.doi.org/10.1111/febs.12790},
  volume       = {281},
  year         = {2014},
}