Ono Eiichiro, Hatayama Masayoshi, Isono Yuri, Sato Takuya, Watanabe Ryoko, Yonekura-Sakakibara Keiko, Fukuchi-Mizutani Masako, Tanaka Yoshikazu, Kusumi Takaaki, Nishino Tokuzo, Nakayama Toru
Suntory Research Center, Shimamoto-cho, Mishima-gun, Osaka 618-8503, Japan.
Plant J. 2006 Jan;45(2):133-43. doi: 10.1111/j.1365-313X.2005.02625.x.
Aureusidin synthase, a polyphenol oxidase (PPO), specifically catalyzes the oxidative formation of aurones from chalcones, which are plant flavonoids, and is responsible for the yellow coloration of snapdragon (Antirrhinum majus) flowers. All known PPOs have been found to be localized in plastids, whereas flavonoid biosynthesis is thought to take place in the cytoplasm [or on the cytoplasmic surface of the endoplasmic reticulum (ER)]. However, the primary structural characteristics of aureusidin synthase and some of its molecular properties argue against localization of the enzyme in plastids and the cytoplasm. In this study, the subcellular localization of the enzyme in petal cells of the yellow snapdragon was investigated. Sucrose-density gradient and differential centrifugation analyses suggested that the enzyme (the 39-kDa mature form) is not located in plastids or on the ER. Transient assays using a green fluorescent protein (GFP) chimera fused with the putative propeptide of the PPO precursor suggested that the enzyme was localized within the vacuole lumen. We also found that the necessary information for vacuolar targeting of the PPO was encoded within the 53-residue N-terminal sequence (NTPP), but not in the C-terminal sequence of the precursor. NTPP-mediated ER-to-Golgi trafficking to vacuoles was confirmed by means of the co-expression of an NTPP-GFP chimera with a dominant negative mutant of the Arabidopsis GTPase Sar1 or with a monomeric red fluorescent protein (mRFP)-fused Golgi marker (an H+-translocating inorganic pyrophosphatase of Arabidopsis). We identified a sequence-specific vacuolar sorting determinant in the NTPP of the precursor. We have demonstrated the biosynthesis of a flavonoid skeleton in vacuoles. The findings of this metabolic compartmentation may provide a strategy for overcoming the biochemical instability of the precursor chalcones in the cytoplasm, thus leading to the efficient accumulation of aurones in the flower.
金黄素合成酶是一种多酚氧化酶(PPO),它特异性地催化查耳酮(一种植物类黄酮)氧化形成金黄酮,该酶还负责金鱼草(Antirrhinum majus)花朵的黄色着色。所有已知的PPO都定位于质体中,而类黄酮生物合成被认为发生在细胞质[或内质网(ER)的细胞质表面]。然而,金黄素合成酶的一级结构特征及其一些分子特性表明该酶并不定位于质体和细胞质中。在本研究中,我们对该酶在黄色金鱼草花瓣细胞中的亚细胞定位进行了研究。蔗糖密度梯度离心和差速离心分析表明,该酶(39 kDa的成熟形式)并不位于质体或内质网上。使用与PPO前体假定前肽融合的绿色荧光蛋白(GFP)嵌合体进行的瞬时分析表明,该酶定位于液泡腔中。我们还发现,PPO靶向液泡的必要信息编码在53个氨基酸的N端序列(NTPP)中,而不是前体的C端序列中。通过将NTPP-GFP嵌合体与拟南芥GTP酶Sar1的显性负突变体或与单体红色荧光蛋白(mRFP)融合的高尔基体标记物(拟南芥的一种H +转运无机焦磷酸酶)共表达,证实了NTPP介导的从内质网到高尔基体再到液泡的运输。我们在前体的NTPP中鉴定出了一个序列特异性的液泡分选决定簇。我们已经证明了液泡中类黄酮骨架的生物合成。这种代谢区室化的发现可能为克服细胞质中前体查耳酮的生化不稳定性提供一种策略,从而导致花朵中金黄酮的有效积累。