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发现并描述了一类参与硫代谢的新型原核纳米结构域家族。

Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism.

机构信息

Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.

Department of Molecular Genetics, University of Toronto, Toronto, Canada.

出版信息

Elife. 2021 Apr 6;10:e59288. doi: 10.7554/eLife.59288.

Abstract

Prokaryotic nanocompartments, also known as encapsulins, are a recently discovered proteinaceous organelle-like compartment in prokaryotes that compartmentalize cargo enzymes. While initial studies have begun to elucidate the structure and physiological roles of encapsulins, bioinformatic evidence suggests that a great diversity of encapsulin nanocompartments remains unexplored. Here, we describe a novel encapsulin in the freshwater cyanobacterium PCC 7942. This nanocompartment is upregulated upon sulfate starvation and encapsulates a cysteine desulfurase enzyme via an N-terminal targeting sequence. Using cryo-electron microscopy, we have determined the structure of the nanocompartment complex to 2.2 Å resolution. Lastly, biochemical characterization of the complex demonstrated that the activity of the cysteine desulfurase is enhanced upon encapsulation. Taken together, our discovery, structural analysis, and enzymatic characterization of this prokaryotic nanocompartment provide a foundation for future studies seeking to understand the physiological role of this encapsulin in various bacteria.

摘要

原核纳米结构域,也被称为被膜小体,是一种在原核生物中最近发现的具有蛋白质细胞器样性质的隔室,能够将货物酶分隔开来。虽然最初的研究已经开始阐明被膜小体的结构和生理作用,但生物信息学证据表明,大量的被膜小体纳米结构域仍未被探索。在这里,我们描述了淡水蓝藻 PCC 7942 中的一种新型被膜小体。这种纳米结构域在硫酸盐饥饿时上调,并通过 N 端靶向序列将半胱氨酸脱硫酶包裹在内。使用冷冻电子显微镜,我们已经确定了纳米结构域复合物的结构分辨率为 2.2 Å。最后,对该复合物的生化特性进行了表征,证明了半胱氨酸脱硫酶的活性在包裹后得到增强。综上所述,我们对这种原核纳米结构域的发现、结构分析和酶学特性的研究为未来研究提供了基础,旨在了解这种被膜小体在各种细菌中的生理作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fbd0/8049743/d880405a0b15/elife-59288-fig1.jpg

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