确定衣藻核糖体生物发生过程中的角色:保守因子 NIP7

IF 2.5 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY Biochimica et biophysica acta. Proteins and proteomics Pub Date : 2024-08-30 DOI:10.1016/j.bbapap.2024.141045
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引用次数: 0

摘要

核糖体生物发生(RB)是真核生物中一个高度保守的过程,它导致功能性核糖体亚基的组装。对酿酒酵母和智人的研究发现了许多 RB 因子(RBFs),包括 NIP7 蛋白,它参与晚期前 60S 核糖体的成熟。在衣藻中也观察到了 NIP7 的表达,凸显了其进化意义。本研究旨在通过蛋白质互补试验和对霉素抗性试验,评估来自莱茵衣藻的 NIP7 蛋白(CrNip7)对酵母中 NIP7 作用的互补能力,从而确定其功能特征。通过酵母双杂交试验进行了蛋白质相互作用研究,以确定 CrNip7 的潜在蛋白质伙伴。此外,还利用 CrNip7 的预测结构进行了 rRNA 建模分析,以研究其与 rRNA 的相互作用。研究发现,CrNip7 可以补充 NIP7 在酵母中的作用,表明 CrNip7 与 60S 核糖体亚基的生物发生有关。此外,通过酵母双杂交实验还发现了CrNip7的两个可能伙伴蛋白UNC-p和G-patch。这些蛋白与CrNip7相互作用的潜力通过硅学分析进行了探讨。此外,还对核酸相互作用进行了评估,结果表明 CrNIP7 的 N 端和 C 端结构域参与了与 rRNA 的相互作用。总之,我们的研究结果为研究 RBFs CrNip7 提供了有价值的见解,为真核模式生物中 RB 的比较研究提供了新的信息,揭示了它在不同物种间的进化保护和功能作用。
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Assigning roles in Chlamydomonas ribosome biogenesis: The conserved factor NIP7

Ribosome biogenesis (RB) is a highly conserved process across eukaryotes that results in the assembly of functional ribosomal subunits. Studies in Saccharomyces cerevisiae and Homo sapiens have identified numerous RB factors (RBFs), including the NIP7 protein, which is involved in late-stage pre-60S ribosomal maturation. NIP7 expression has also been observed in Chlamydomonas reinhardtii, highlighting its evolutionary significance. This study aimed to characterize the function of the NIP7 protein from C. reinhardtii (CrNip7) through protein complementation assays and a paromomycin resistance test, assessing its ability to complement the role of NIP7 in yeast. Protein interaction studies were conducted via yeast two-hybrid assay to identify potential protein partners of CrNip7. Additionally, rRNA modeling analysis was performed using the predicted structure of CrNip7 to investigate its interaction with rRNA. The study revealed that CrNip7 can complement the role of NIP7 in yeast, implicating CrNip7 in the biogenesis of the 60S ribosomal subunit. Furthermore, two possible partner proteins of CrNip7, UNC-p and G-patch, were identified through yeast two-hybrid assay. The potential of these proteins to interact with CrNip7 was explored through in silico analyses. Furthermore, nucleic acid interaction was also evaluated, indicating the involvement of the N- and C-terminal domains of CrNIP7 in interacting with rRNA. Collectively, our findings provide valuable insights into the RBFs CrNip7, offering novel information for comparative studies on RB among eukaryotic model organisms, shedding light on its evolutionary conservation and functional role across species.

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来源期刊
CiteScore
8.00
自引率
0.00%
发文量
55
审稿时长
33 days
期刊介绍: BBA Proteins and Proteomics covers protein structure conformation and dynamics; protein folding; protein-ligand interactions; enzyme mechanisms, models and kinetics; protein physical properties and spectroscopy; and proteomics and bioinformatics analyses of protein structure, protein function, or protein regulation.
期刊最新文献
Serratiopeptidase exhibits antibiofilm activity through the proteolytic function of N-terminal domain and versatile function of the C-terminal domain Assigning roles in Chlamydomonas ribosome biogenesis: The conserved factor NIP7 From sequence to function: Exploring biophysical properties of bacteriophage BFK20 lytic transglycosylase domain from the minor tail protein gp15 Identification of potential pharmacological chaperones that selectively stabilize mutated Aspartoacylases in Canavan disease Editorial Board
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