The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.)
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8001695
- author
- Bollivar, D. ; Braumann, I. ; Berendt, K. ; Gough, S. P. and Hansson, Mats LU
- publishing date
- 2014
- 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
- Wiley-Blackwell
- external identifiers
-
- scopus:84901233802
- pmid:24661504
- ISSN
- 1742-464X
- DOI
- 10.1111/febs.12790
- language
- English
- LU publication?
- no
- additional info
- 10
- id
- 7f2cebc2-d4d7-4871-8560-0aa1614ad6f9 (old id 8001695)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24661504
- date added to LUP
- 2016-04-01 10:00:23
- date last changed
- 2022-01-25 18:49:21
@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}}, 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}}, language = {{eng}}, number = {{10}}, pages = {{2377--2386}}, publisher = {{Wiley-Blackwell}}, 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}}, doi = {{10.1111/febs.12790}}, volume = {{281}}, year = {{2014}}, }