Vega-Cabrera Luz Adriana, Wood Christopher D, Pardo-López Liliana
Instituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad #2001, Apdo. Postal 510-3, 62250, Cuernavaca, Morelos, Mexico.
Laboratorio Nacional de Microscopía Avanzada, Universidad Nacional Autónoma de México, Av. Universidad #2001, Apdo. Postal 510-3, 62250, Cuernavaca, Morelos, Mexico.
Curr Genet. 2018 Feb;64(1):17-23. doi: 10.1007/s00294-017-0718-3. Epub 2017 Jun 2.
In this mini-review, we present a perspective on the recent findings relating Spo0M structure and function that will stimulate and guide further studies in the characterization of this interesting protein. Cell division and sporulation constitute two of the best studied processes in the model organism Bacillus subtilis; however, there are many missing pieces in the giant regulatory puzzle that governs the independent and shared networks between them. Spo0M is a little studied protein that has been related to both, cell division and sporulation, but its biochemical function and its direct interactions have not been yet defined. Structural analysis of Spo0M revealed the presence of an arrestin-like domain and an FP domain (a dimerization domain present in proteasome elements), motifs more commonly found in eukaryotic proteins. The aim of this perspective is to present open questions regarding the functional and structural features of Spo0M that make this protein a good candidate for the ancestor of arrestins in bacteria and an important element in developmental and differentiation processes of Bacillus subtilis.
在本综述中，我们就近期关于Spo0M结构与功能的研究发现提出一种观点，这将激发并指导对这种有趣蛋白质特性的进一步研究。细胞分裂和芽孢形成是模式生物枯草芽孢杆菌中研究得最为深入的两个过程；然而，在支配它们之间独立和共享网络的庞大调控谜题中，仍存在许多缺失环节。Spo0M是一种研究较少的蛋白质，它与细胞分裂和芽孢形成均有关联，但其生化功能及其直接相互作用尚未明确。对Spo0M的结构分析揭示了一个类抑制蛋白结构域和一个FP结构域（一种存在于蛋白酶体元件中的二聚化结构域），这些基序在真核生物蛋白质中更为常见。本观点的目的是提出有关Spo0M功能和结构特征的开放性问题，这些问题使该蛋白质成为细菌中抑制蛋白祖先的良好候选者以及枯草芽孢杆菌发育和分化过程中的重要元件。
