The complex domain architecture of SAMD9 family proteins, predicted STAND-like NTPases, suggests new links to inflammation and apoptosis.

The complex domain architecture of SAMD9 family proteins, predicted STAND-like NTPases, suggests new links to inflammation and apoptosis.
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DOI:
10.1186/s13062-017-0185-2
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发表时间:
2017-05-25
期刊:
影响因子:
5.5
通讯作者:
Koonin EV
Koonin EV
中科院分区:
生物学2区
文献类型:
--
作者:
Mekhedov SL;Makarova KS;Koonin EV

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我们报告了一个全面的计算解剖的域结构的SAMD 9家族蛋白,参与在人类的抗病毒和抗肿瘤反应。我们表明,SAMD 9蛋白家族在大多数动物中都有代表性,而且出乎意料地,在细菌中,特别是放线菌中。从N末端到C末端,核心SAMD 9家族结构包括DNA/RNA结合AlbA结构域、变体Sir 2样结构域、STAND样P环NTPase、TPR重复序列阵列和具有预测RNA结合特性的OB折叠结构域。脊椎动物SAMD 9家族蛋白含有能够聚合的epidermal SAM结构域,而来自其他动物的一些家族成员则含有DEATH超家族的同型衔接子结构域,称为凋亡网络的专用组分。这种复杂的结构域结构让人想起STAND超家族NTPases,其参与真核生物和原核生物中的各种信号传导过程,包括程序性细胞死亡。这些发现表明,SAMD 9是一个新的、进化上保守的防御网络的枢纽,其特征仍有待描述。本文由Igor B审阅。朱琳和门苏尔·德拉基奇。本文的在线版本(doi:10.1186/s13062-017-0185-2)包含补充材料,可供授权用户使用。
We report a comprehensive computational dissection of the domain architecture of the SAMD9 family proteins that are involved in antivirus and antitumor response in humans. We show that the SAMD9 protein family is represented in most animals and also, unexpectedly, in bacteria, in particular actinomycetes. From the N to C terminus, the core SAMD9 family architecture includes DNA/RNA-binding AlbA domain, a variant Sir2-like domain, a STAND-like P-loop NTPase, an array of TPR repeats and an OB-fold domain with predicted RNA-binding properties. Vertebrate SAMD9 family proteins contain the eponymous SAM domain capable of polymerization, whereas some family members from other animals instead contain homotypic adaptor domains of the DEATH superfamily, known as dedicated components of apoptosis networks. Such complex domain architecture is reminiscent of the STAND superfamily NTPases that are involved in various signaling processes, including programmed cell death, in both eukaryotes and prokaryotes. These findings suggest that SAMD9 is a hub of a novel, evolutionarily conserved defense network that remains to be characterized. This article was reviewed by Igor B. Zhulin and Mensur Dlakic. The online version of this article (doi:10.1186/s13062-017-0185-2) contains supplementary material, which is available to authorized users.