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The Y cf54 protein is part of the membrane component of M g‐protoporphyrin IX monomethyl ester cyclase from barley ( H ordeum vulgare L .)
Author(s) -
Bollivar David,
Braumann Ilka,
Berendt Kasper,
Gough Simon P.,
Hansson Mats
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12790
Subject(s) - enzyme , cyclase , plastid , biochemistry , chemistry , biosynthesis , membrane , biology , chloroplast , gene
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, X anL, is found associated with the membrane and another protein, Y cf54, has recently been identified based upon association with X an L . This study describes a deeper analysis of the role of Y cf54 in the enzyme and the localization of the protein in barley plastids. The results clearly demonstrate a strong association of Y cf54 with X anL, absence of Y cf54 from soluble fractions necessary for activity and more evidence for a third membrane localized component of the enzyme. Structured digital abstract Ycf54 and Ycf54 bind by molecular sieving ( 1 , 2 )