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

Standard

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.; Hansson, Mats.

In: The FEBS Journal, Vol. 281, No. 10, 2014, p. 2377-2386.

Research output: Contribution to journalArticle

Harvard

APA

CBE

MLA

Vancouver

Author

RIS

TY - JOUR

T1 - The Ycf54 protein is part of the membrane component of Mg-protoporphyrin IX monomethyl ester cyclase from barley (Hordeum vulgare L.)

AU - Bollivar, D.

AU - Braumann, I.

AU - Berendt, K.

AU - Gough, S. P.

AU - Hansson, Mats

N1 - 10

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

KW - Mg-protoporphyrin monomethyl ester

KW - Protoporphyrins/metabolism

KW - Plastids/metabolism

KW - Plant Proteins/chemistry/genetics/metabolism

KW - Oxygenases/chemistry/genetics/metabolism

KW - Mutation

KW - Plant

KW - Genes

KW - Hordeum/genetics/metabolism

KW - chlorophyll

KW - cyclase

KW - etioplast

KW - isocyclic ring

U2 - 10.1111/febs.12790

DO - 10.1111/febs.12790

M3 - Article

VL - 281

SP - 2377

EP - 2386

JO - The FEBS Journal

T2 - The FEBS Journal

JF - The FEBS Journal

SN - 1742-464X

IS - 10

ER -