Department of Biology, Illinois Wesleyan University, Bloomington, IL, USA.
FEBS J. 2014 May;281(10):2377-86. doi: 10.1111/febs.12790. Epub 2014 Apr 7.
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.
叶绿素的生物合成被证明需要一整套酶,其初始阶段与血红素的合成共享。在这些酶中,最神秘的是 Mg-原卟啉 IX 单甲酯环化酶(EC 1.14.13.81)。该酶需要与质体膜和质体可溶性部分相关联的成分。其中一种成分 XanL 与膜相关联,另一种蛋白质 Ycf54 最近根据与 XanL 的关联而被鉴定出来。本研究描述了对 Ycf54 在酶中的作用以及该蛋白在大麦质体中的定位的更深入分析。结果清楚地表明 Ycf54 与 XanL 有很强的关联,Ycf54 不存在于活性必需的可溶性部分中,并且有更多证据表明该酶还有第三个定位于膜的成分。