Classification of the caspase-hemoglobinase fold: Detection of new families and implications for the origin of the eukaryotic separins
Classification of the caspase-hemoglobinase fold: Detection of new families and implications for the origin of the eukaryotic separins
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DOI：
10.1002/prot.10060
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发表时间：
2002-03-01
影响因子：
2.9
通讯作者：
Koonin, EV
中科院分区：
文献类型：
--
作者：
Aravind, L;Koonin, EV
一个全面的序列和结构的比较分析的半胱天冬酶，血红蛋白酶，蛋白折叠导致的蛋白酶结构域的最小结构核心的划定和许多以前未检测到的成员，包括一个新的蛋白酶家族的HetF蛋白为代表的蓝藻念珠藻的鉴定。豆类和血红蛋白酶的第一个细菌同源物也被确定。大多数含有该折叠的蛋白是已知的或预测为活性蛋白酶，但在几乎所有谱系中都注意到多个独立的失活。再加上半胱天冬酶相关蛋白酶形成分子内或分子间二聚体的趋势，这表明无活性形式具有广泛的调节作用。半胱天冬酶-血红蛋白酶折叠的分类，以反映推断的组成蛋白质家族之间的进化关系。迄今为止，几乎只在细菌和真核生物中检测到含有该结构域的蛋白质。这一分析表明，胱天蛋白酶-血红蛋白酶-折叠蛋白酶及其失活衍生物广泛存在于各种细菌中，特别是那些具有复杂发育的细菌，如链霉菌属、鱼腥藻属、中生根瘤菌属和粘球菌属。真核分离蛋白家族与主要的原核HetF家族关系最为密切。这些蛋白质之间的系统模式和进化关系表明，它们可能是由真核生物在原线粒体内共生过程中从细菌中获得的。一个类似的情况下，支持系统发育分析，似乎适用于metacaspase和paracaspase，后者，也许，被收购在一个独立的水平转移到真核生物。真核生物获得半胱天冬酶-血红蛋白酶-折叠结构域可能在重要的真核生物过程的进化中至关重要，如有丝分裂和程序性细胞死亡。(C)2002 Wiley-Liss，Inc.
A comprehensive sequence and structural comparative analysis of the caspase-hemoglobinase, protein fold resulted in the delineation of the minimal structural core of the protease domain and the identification of numerous, previously undetected members, including a new protease family typified by the HetF protein from the cyanobacterium Nostoc. The first bacterial homologs of legumains and hemoglobinases were also identified. Most proteins containing this fold are known or predicted to be active proteases, but multiple, independent inactivations were noticed in nearly all lineages. Together with the tendency of caspase-related proteases to form intramolecular or intermolecular dimers, this suggests a widespread regulatory role for the inactive forms. A classification of the caspase-hemoglobinase fold was developed to reflect the inferred evolutionary relationships between the constituent protein families. Proteins containing this domain were so far detected almost exclusively in bacteria and eukaryotes. This analysis indicates that caspase-hemoglobinase-fold proteases and their inactivated derivatives are widespread in diverse bacteria, particularly those with a complex development, such as Streptomyces, Anabaena, Mesorhizobium, and Myxococcus. The eukaryotic separin family was shown to be most closely related to the mainly prokaryotic HetF family. The phyletic patterns and evolutionary relationships between these proteins suggest that they probably were acquired by eukaryotes from bacteria during the primary, promitochondrial endosymbiosis. A similar scenario, supported by phylogenetic analysis, seems to apply to metacaspases and paracaspases, with the latter, perhaps, being acquired in an independent horizontal transfer to the eukaryotes. The acquisition of the caspase-hemoglobinase-fold domains by eukaryotes might have been critical in the evolution of important eukaryotic processes, such as mitosis and programmed cell death. (C) 2002 Wiley-Liss, Inc.