Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis.
Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis.
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DOI：
10.1016/j.jbc.2021.100338
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发表时间：
2021-01
期刊：
影响因子：
--
通讯作者：
van Wijk KJ
中科院分区：
文献类型：
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作者：
Bouchnak I;van Wijk KJ
与不同细胞活动相关的ATPase(AAA+)是一个蛋白质超家族，通常组装成六聚体环。这些蛋白质含有AAA+结构域，具有两个典型的基序(Walker A和B)，可以结合和水解ATP，使它们能够执行各种不同的功能。例如，AAA+蛋白通过控制细胞内存在的蛋白质的生物发生、折叠、运输和降解，在细胞蛋白稳定中发挥着重要作用。几个中央蛋白分解系统(如CLP、DIG、FtsH、LON、26S蛋白酶体)利用AAA+结构域或AAA+蛋白质(利用来自ATP水解的能量)来展开蛋白质底物，使它们能够被降解。这使得AAA+蛋白酶系统可以降解聚集体和大蛋白质，以及小蛋白质，并将它们作为线性化分子送入蛋白酶小室。本文综述了蓝藻(如聚球藻)、光合作用真核生物(如拟南芥、衣藻)和非光合性恶性疟原虫原生质外体中必需的CLP AAA+蛋白水解酶系统的最新进展和比较概况。重点介绍了在鉴定CLP蛋白酶结构、底物、底物接头(如NblA/B、CLPs、ClpF)和降解方面的最新进展和突破。我们评论了CLP活性的生理重要性，包括叶绿体生物发生、蛋白稳定、叶绿体蛋白展开反应和代谢，跨越这些不同的谱系。讨论了悬而未决的问题以及更好地了解CLP系统在细胞蛋白稳态中的基本作用的研究机会和优先事项。
ATPases Associated with diverse cellular Activities (AAA+) are a superfamily of proteins that typically assemble into hexameric rings. These proteins contain AAA+ domains with two canonical motifs (Walker A and B) that bind and hydrolyze ATP, allowing them to perform a wide variety of different functions. For example, AAA+ proteins play a prominent role in cellular proteostasis by controlling biogenesis, folding, trafficking, and degradation of proteins present within the cell. Several central proteolytic systems (e.g., Clp, Deg, FtsH, Lon, 26S proteasome) use AAA+ domains or AAA+ proteins to unfold protein substrates (using energy from ATP hydrolysis) to make them accessible for degradation. This allows AAA+ protease systems to degrade aggregates and large proteins, as well as smaller proteins, and feed them as linearized molecules into a protease chamber. This review provides an up-to-date and a comparative overview of the essential Clp AAA+ protease systems in Cyanobacteria (e.g., Synechocystis spp), plastids of photosynthetic eukaryotes (e.g., Arabidopsis, Chlamydomonas), and apicoplasts in the nonphotosynthetic apicomplexan pathogen Plasmodium falciparum. Recent progress and breakthroughs in identifying Clp protease structures, substrates, substrate adaptors (e.g., NblA/B, ClpS, ClpF), and degrons are highlighted. We comment on the physiological importance of Clp activity, including plastid biogenesis, proteostasis, the chloroplast Protein Unfolding Response, and metabolism, across these diverse lineages. Outstanding questions as well as research opportunities and priorities to better understand the essential role of Clp systems in cellular proteostasis are discussed.