Paulette Sofía Romero-Pérez, Laura V Martínez-Castro, Alejandro Linares, Inti Arroyo-Mosso, Nuria Sánchez-Puig, Cesar L Cuevas-Velazquez, Shahar Sukenik, Adán Guerrero, Alejandra A Covarrubias
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引用次数: 0
摘要
在种子成熟过程中,植物可能会经历严重的干燥,从而导致胚胎发生后期大量蛋白(LEA)的积累。在缺水情况下,这些内在无序蛋白也会在植物组织中积累。体外研究提出了 LEA 蛋白的功能作用,其中单体被认为是功能单位。然而,对于同源异构体的潜在形成却鲜有研究。在这项工作中,我们采用体外和体内方法研究了拟南芥第 4 组 LEA 蛋白(AtLEA4)潜在的自结合。由于 LEA4 蛋白在整个植物王国中的高度保守性,它们是一个引人注目的研究案例。与高度紊乱和低保守的 C 端区域相比,该蛋白家族的特点是 N 端区域保守,具有高的α-螺旋倾向和体内保护活性。我们的研究结果表明,全长 AtLEA4 蛋白会发生寡聚,而且两个末端区域都足以在体外进行自我结合。然而,AtLEA4-5的氨基区和羧基区在体内自结合的能力明显低于整个蛋白质。利用高分辨率和定量荧光显微镜,我们得以揭示 LEA 蛋白在植物体内形成高阶寡聚体的未报道能力。此外,我们还发现高阶复合体需要两个末端区域同时参与,这表明需要整个蛋白质才能实现这种结构组织。这项研究为了解植物中 LEA 蛋白的自我结合提供了宝贵的见解,并强调了蛋白质寡聚体形成的作用。
Self-association and multimer formation in AtLEA4-5, a desiccation-induced intrinsically disordered protein from plants.
During seed maturation, plants may experience severe desiccation, leading to the accumulation of late embryogenesis abundant (LEA) proteins. These intrinsically disordered proteins also accumulate in plant tissues under water deficit. Functional roles of LEA proteins have been proposed based on in vitro studies, where monomers are considered as the functional units. However, the potential formation of homo-oligomers has been little explored. In this work, we investigated the potential self-association of Arabidopsis thaliana group 4 LEA proteins (AtLEA4) using in vitro and in vivo approaches. LEA4 proteins represent a compelling case of study due to their high conservation throughout the plant kingdom. This protein family is characterized by a conserved N-terminal region, with a high alpha-helix propensity and invitro protective activity, as compared to the highly disordered and low-conserved C-terminal region. Our findings revealed that full-length AtLEA4 proteins oligomerize and that both terminal regions are sufficient for self-association in vitro. However, the ability of both amino and carboxy regions of AtLEA4-5 to self-associate invivo is significantly lower than that of the entire protein. Using high-resolution and quantitative fluorescence microscopy, we were able to disclose the unreported ability of LEA proteins to form high-order oligomers in planta. Additionally, we found that high-order complexes require the simultaneous engagement of both terminal regions, indicating that the entire protein is needed to attain such structural organization. This research provides valuable insights into the self-association of LEA proteins in plants and emphasizes the role of protein oligomer formation.
期刊介绍:
Protein Science, the flagship journal of The Protein Society, is a publication that focuses on advancing fundamental knowledge in the field of protein molecules. The journal welcomes original reports and review articles that contribute to our understanding of protein function, structure, folding, design, and evolution.
Additionally, Protein Science encourages papers that explore the applications of protein science in various areas such as therapeutics, protein-based biomaterials, bionanotechnology, synthetic biology, and bioelectronics.
The journal accepts manuscript submissions in any suitable format for review, with the requirement of converting the manuscript to journal-style format only upon acceptance for publication.
Protein Science is indexed and abstracted in numerous databases, including the Agricultural & Environmental Science Database (ProQuest), Biological Science Database (ProQuest), CAS: Chemical Abstracts Service (ACS), Embase (Elsevier), Health & Medical Collection (ProQuest), Health Research Premium Collection (ProQuest), Materials Science & Engineering Database (ProQuest), MEDLINE/PubMed (NLM), Natural Science Collection (ProQuest), and SciTech Premium Collection (ProQuest).