Novel G-protein-coupled receptor-like proteins in the plant pathogenic fungus Magnaporthe grisea.

Novel G-protein-coupled receptor-like proteins in the plant pathogenic fungus Magnaporthe grisea.
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DOI:
10.1186/gb-2005-6-3-r24
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发表时间:
2005
期刊:
影响因子:
12.3
通讯作者:
Dean RA
Dean RA
中科院分区:
生物学1区
文献类型:
--
作者:
Kulkarni RD;Thon MR;Pan H;Dean RA

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对稻瘟病菌基因组的分析以及与其他真菌的比较,鉴定出已知的 G 蛋白偶联受体样蛋白的同源物和稻瘟病菌中一类新的 GPCR 样受体,它们是丝状子囊菌真菌特有的。 G 蛋白偶联受体 (GPCR) 是人类和其他动物基因组中最大的蛋白质家族之一,但在真菌中鉴定的 GPCR 不超过 10 个。真菌只含有这么少量的受体还是还有更多的受体有待发现?我们利用最近测序的真菌植物病原体稻瘟病菌的基因组提出了这个问题。在稻瘟病菌中鉴定出与真菌特异性和其他真核 GPCR 具有显着相似性的蛋白质。这些包括已知真菌 GPCR 的同源物、盘基网柄菌的 cAMP 受体和类固醇受体 mPR。我们还发现了一类以 PTH11 为代表的新型受体,PTH11 是致病性所需的细胞表面整合膜蛋白。 PTH11 具有七个跨膜区域和一个氨基末端富含半胱氨酸的 EGF 样结构域(CFEM 结构域),这一特征在人类 GPCR 中也可见。在稻瘟病菌中鉴定出 61 个 PTH11 相关蛋白,它们与粗糙脉孢菌和属于子囊菌亚门(盘菌亚门)的其他真菌中的同源物具有共同的结构域。在其他真菌类群(担子菌门或其他子囊菌亚门,包括酵母)或任何其他真核生物中均未检测到。包含 CFEM 结构域的 PTH11 亚类在稻瘟病菌中具有高度代表性。在稻瘟病菌中,我们鉴定了已知 GPCR 的同源物和丝状子囊菌特异的一类新型 GPCR 样受体。这一新类别的成员 PTH11 是发病机制所必需的,因此表明其他成员在致病性中也发挥着作用。所鉴定的类别构成了迄今为止在真菌中报道的最多数量的 GPCR 样蛋白。
An analysis of the Magnaporthe grisea genome and comparison with other fungi identified homologs of known G protein-coupled receptor-like proteins and a novel class of GPCR-like receptors in M. grisea that are specific to filamentous ascomycete fungi. The G-protein-coupled receptors (GPCRs) are one of the largest protein families in human and other animal genomes, but no more than 10 GPCRs have been characterized in fungi. Do fungi contain only this handful or are there more receptors to be discovered? We asked this question using the recently sequenced genome of the fungal plant pathogen Magnaporthe grisea. Proteins with significant similarity to fungus-specific and other eukaryotic GPCRs were identified in M. grisea. These included homologs of known fungal GPCRs, the cAMP receptors from Dictyostelium, and a steroid receptor mPR. We also identified a novel class of receptors typified by PTH11, a cell-surface integral membrane protein required for pathogenicity. PTH11 has seven transmembrane regions and an amino-terminal extracellular cysteine-rich EGF-like domain (CFEM domain), a characteristic also seen in human GPCRs. Sixty-one PTH11-related proteins were identified in M. grisea that shared a common domain with homologs in Neurospora crassa and other fungi belonging to this subphylum of the Ascomycota (the Pezizomycotina). None was detected in other fungal groups (Basidiomycota or other Ascomycota subphyla, including yeasts) or any other eukaryote. The subclass of PTH11 containing the CFEM domain is highly represented in M. grisea. In M. grisea we identified homologs of known GPCRs and a novel class of GPCR-like receptors specific to filamentous ascomycetes. A member of this new class, PTH11, is required for pathogenesis, thus suggesting roles in pathogenicity for other members. The identified classes constitute the largest number of GPCR-like proteins reported in fungi to date.
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