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子囊菌粘附蛋白的分子系统发育——裂殖酵母中一类假定的细胞表面粘附蛋白新家族。

Molecular phylogenetics of ascomycotal adhesins--a novel family of putative cell-surface adhesive proteins in fission yeasts.

作者信息

Linder Tomas, Gustafsson Claes M

机构信息

Division of Metabolic Diseases, Karolinska Institutet, Novum, SE-141 86 Stockholm, Sweden.

出版信息

Fungal Genet Biol. 2008 Apr;45(4):485-97. doi: 10.1016/j.fgb.2007.08.002. Epub 2007 Aug 17.

DOI:10.1016/j.fgb.2007.08.002
PMID:17870620
Abstract

In this work, we identify a family of putative adhesins in the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. The members of this family share a conserved tandem repeat related to those found in the Candida albicans Als family of adhesins. Unlike previously characterised adhesins that possess conserved ligand-binding domains at the N-terminus, this group of proteins carry ligand-binding domains at their C-termini. We demonstrate that one such domain--the uncharacterised GLEYA domain, is related to the lectin-like ligand-binding domain found in the Saccharomyces cerevisiae Flo proteins. Unlike the Flo and Als proteins, the fission yeast adhesins do not contain detectable glycosyl phosphatidyl inositol (GPI) membrane anchor signals to mediate their attachment to the cell wall, which may suggest a novel cell wall attachment mechanism. Further sequence analysis identified several putative adhesins in the sub-phylum of Pezizomycotina, where only a few adhesins have been described to date.

摘要

在这项研究中,我们在粟酒裂殖酵母和日本裂殖酵母中鉴定出一个假定的粘附素家族。该家族成员共享一个保守的串联重复序列,与白色念珠菌Als粘附素家族中发现的那些序列相关。与之前在N端具有保守配体结合结构域的已鉴定粘附素不同,这组蛋白在其C端携带配体结合结构域。我们证明,其中一个这样的结构域——未表征的GLEYA结构域,与酿酒酵母Flo蛋白中发现的凝集素样配体结合结构域相关。与Flo和Als蛋白不同,裂殖酵母粘附素不包含可检测到的糖基磷脂酰肌醇(GPI)膜锚信号来介导它们与细胞壁的附着,这可能暗示了一种新的细胞壁附着机制。进一步的序列分析在盘菌亚门中鉴定出几种假定的粘附素,迄今为止,该亚门中仅描述了少数几种粘附素。

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