Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.

Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.
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DOI:
10.1002/prot.26204
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发表时间:
2022-01
期刊:
影响因子:
2.9
通讯作者:
Pornillos O
Pornillos O
中科院分区:
生物学4区
文献类型:
--
作者:
Zurowska K;Alam A;Ganser-Pornillos BK;Pornillos O

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逆转录病毒的Gag蛋白通过形成蛋白质外壳或衣壳,从而产生病毒粒子室,在病毒颗粒组装中起重要作用。现在已经鉴定出多种人类蛋白质具有一个或多个主要Gag结构域的结构相似性。这些人类蛋白质被认为是从由逆转录病毒感染或反转录转座子引起的古代整合进化或“驯化”的。在这里,我们报道了MOAP1(凋亡调节因子1)和PEG10(父系表达基因10)的稳定折叠结构域的x射线晶体结构与同源Gag蛋白的c端衣壳(CA)结构域高度相似。这些结构证实了MOAP1和PEG10被归类为驯化的gag,并表明这些蛋白质可能保留了一些促进其祖先gag组装成衣壳的关键相互作用。
The Gag proteins of retroviruses play an essential role in virus particle assembly by forming a protein shell or capsid and thus generating the virion compartment. A variety of human proteins have now been identified with structural similarity to one or more of the major Gag domains. These human proteins are thought to have been evolved or “domesticated” from ancient integrations due to retroviral infections or retrotransposons. Here, we report that X-ray crystal structures of stably folded domains of MOAP1 (modulator of apoptosis 1) and PEG10 (paternally expressed gene 10) are highly similar to the C-terminal capsid (CA) domains of cognate Gag proteins. The structures confirm classification of MOAP1 and PEG10 as domesticated Gags, and suggest that these proteins may have preserved some of the key interactions that facilitated assembly of their ancestral Gags into capsids.
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