Dipartimento di Agrobiologia e Agrochimica, Università della Tuscia, Via S, Camillo De Lellis, 01100 Viterbo, Italy.
BMC Plant Biol. 2010 Jun 3;10:101. doi: 10.1186/1471-2229-10-101.
The Protein Disulfide Isomerase (PDI) gene family encodes several PDI and PDI-like proteins containing thioredoxin domains and controlling diversified metabolic functions, including disulfide bond formation and isomerisation during protein folding. Genomic, cDNA and promoter sequences of the three homologous wheat genes encoding the "typical" PDI had been cloned and characterized in a previous work. The purpose of present research was the cloning and characterization of the complete set of genes encoding PDI and PDI like proteins in bread wheat (Triticum aestivum cv Chinese Spring) and the comparison of their sequence, structure and expression with homologous genes from other plant species.
Eight new non-homologous wheat genes were cloned and characterized. The nine PDI and PDI-like sequences of wheat were located in chromosome regions syntenic to those in rice and assigned to eight plant phylogenetic groups. The nine wheat genes differed in their sequences, genomic organization as well as in the domain composition and architecture of their deduced proteins; conversely each of them showed high structural conservation with genes from other plant species in the same phylogenetic group. The extensive quantitative RT-PCR analysis of the nine genes in a set of 23 wheat samples, including tissues and developmental stages, showed their constitutive, even though highly variable expression.
The nine wheat genes showed high diversity, while the members of each phylogenetic group were highly conserved even between taxonomically distant plant species like the moss Physcomitrella patens. Although constitutively expressed the nine wheat genes were characterized by different expression profiles reflecting their different genomic organization, protein domain architecture and probably promoter sequences; the high conservation among species indicated the ancient origin and diversification of the still evolving gene family. The comprehensive structural and expression characterization of the complete set of PDI and PDI-like wheat genes represents a basis for the functional characterization of this gene family in the hexaploid context of bread wheat.
蛋白质二硫键异构酶(PDI)基因家族编码几种包含硫氧还蛋白结构域的 PDI 和 PDI 样蛋白,控制多样化的代谢功能,包括蛋白质折叠过程中的二硫键形成和异构化。在之前的研究中,已经克隆和表征了编码“典型”PDI 的三个同源小麦基因的基因组、cDNA 和启动子序列。本研究的目的是克隆和表征面包小麦(Triticum aestivum cv Chinese Spring)中编码 PDI 和 PDI 样蛋白的整套基因,并比较它们与其他植物物种同源基因的序列、结构和表达。
克隆并表征了 8 个新的非同源小麦基因。小麦的 9 个 PDI 和 PDI 样序列位于与水稻同源的染色体区域,并被分配到 8 个植物系统发育群中。这 9 个小麦基因在序列、基因组组织以及它们推导的蛋白质的结构域组成和结构上存在差异;相反,它们中的每一个都与同一系统发育群中来自其他植物物种的基因表现出高度的结构保守性。对 23 个小麦样本(包括组织和发育阶段)的 9 个基因进行了广泛的定量 RT-PCR 分析,结果表明它们的表达是组成型的,尽管变化很大。
这 9 个小麦基因表现出高度的多样性,而每个系统发育群的成员在分类上相距甚远的植物物种之间(如苔藓 Physcomitrella patens)也表现出高度的保守性。尽管这 9 个小麦基因表达是组成型的,但它们的表达谱不同,反映了它们不同的基因组组织、蛋白质结构域结构和可能的启动子序列;物种间的高度保守性表明该基因家族具有古老的起源和多样化的进化历程。完整的 PDI 和 PDI 样小麦基因的综合结构和表达特征为在六倍体面包小麦的背景下对该基因家族的功能特征进行研究提供了基础。