Freitag Michael
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331-7305
Mycologia. 2016 May-Jun;108(3):485-505. doi: 10.3852/15-182. Epub 2016 Feb 23.
Chromosome segregation relies on coordinated activity of a large assembly of proteins, the kinetochore interaction network (KIN). How conserved the underlying mechanisms driving the epigenetic phenomenon of centromere and kinetochore assembly and maintenance are remains unclear, even though various eukaryotic models have been studied. More than 50 different proteins, many in multiple copies, comprise the KIN or are associated with fungal centromeres and kinetochores. Proteins isolated from immune sera recognized centromeric regions on chromosomes and thus were named centromere proteins (CENPs). CENP-A, sometimes called centromere-specific H3 (CenH3), is incorporated into nucleosomes within or near centromeres. The constitutive centromere-associated network (CCAN) assembles on this specialized chromatin, likely based on specific interactions with and requiring presence of CENP-C. The outer kinetochore comprises the Knl1-Mis12-Ndc80 (KMN) protein complexes that connect CCAN to spindles, accomplished by binding and stabilizing microtubules (MTs) and in the process generating load-bearing assemblies for chromatid segregation. In most fungi the Dam1/DASH complex connects the KMN complexes to MTs. Fungi present a rich resource to investigate mechanistic commonalities but also differences in kinetochore architecture. While ascomycetes have sets of CCAN and KMN proteins that are conserved with those of budding yeast or metazoans, searching other major branches of the fungal kingdom revealed that CCAN proteins are poorly conserved at the primary sequence level. Several conserved binding motifs or domains within KMN complexes have been described recently, and these features of ascomycete KIN proteins are shared with most metazoan proteins. In addition, several ascomycete-specific domains have been identified here.
染色体分离依赖于大量蛋白质组成的复合体——动粒相互作用网络(KIN)的协同活动。尽管已经对多种真核生物模型进行了研究,但驱动着丝粒和动粒组装与维持这一表观遗传现象的潜在机制在多大程度上保守仍不清楚。50多种不同的蛋白质(其中许多是多个拷贝)组成了KIN,或者与真菌着丝粒和动粒相关。从免疫血清中分离出的蛋白质能识别染色体上的着丝粒区域,因此被命名为着丝粒蛋白(CENPs)。CENP-A有时也被称为着丝粒特异性H3(CenH3),它被整合到着丝粒内部或附近的核小体中。组成型着丝粒相关网络(CCAN)在这种特殊的染色质上组装,可能基于与CENP-C的特定相互作用且需要CENP-C的存在。动粒外层由Knl1-Mis12-Ndc80(KMN)蛋白复合体组成,这些复合体将CCAN与纺锤体连接起来,通过结合并稳定微管(MTs)来实现,在此过程中为染色单体分离产生承载组件。在大多数真菌中,Dam1/DASH复合体将KMN复合体与MTs连接起来。真菌为研究动粒结构的机制共性和差异提供了丰富的资源。虽然子囊菌的CCAN和KMN蛋白集与芽殖酵母或后生动物的保守,但在真菌界的其他主要分支中搜索发现,CCAN蛋白在一级序列水平上保守性较差。最近已经描述了KMN复合体中的几个保守结合基序或结构域,子囊菌KIN蛋白的这些特征与大多数后生动物蛋白相同。此外,这里还鉴定出了几个子囊菌特异性结构域。