Arabidopsis transmembrane proteins regulate protein turnover as signaling molecules during internalization by means of ubiquitination

Lin Wang

Abstract


This study attempts to characterize the structure, function, and other features of Arabidopsis thaliana based on its transmembrane protein amino acid sequence and assess its potential as a drug target and ubiquitination site. The transmembrane protein belongs to the Arabidopsis plant, but little is known about the structure-function of the protein, among others. We predicted the structure and transmembrane domains of the transmembrane protein by different bioinformatic tools, and the prediction results showed that its three poorly conserved transmembrane domains could be used as potential drug targeting sites. Among them, lysine ubiquitination sites play an important role in the recycling of plant membrane proteins, and we found the existence of ubiquitination sites by predicting the ubiquitination sites of transmembrane proteins, and this could be a new research direction in the future.


Keywords


domain; multiple alignments; structure prediction; protein ubiquitination sites

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References


Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature. 2000; 408(6814): 796–815. doi: 10.1038/35048692

Ikeda F, Dikic I. Atypical ubiquitin chains: new molecular signals. EMBO reports. 2008; 9(6): 536–542. doi: 10.1038/embor.2008.93

Kölling R, Losko S. The linker region of the ABC-transporter Ste6 mediates ubiquitination and fast turnover of the protein. The EMBO Journal. 1997; 16(9): 2251–2261. doi: 10.1093/emboj/16.9.2251

Barberon M, Zelazny E, Robert S, et al. Monoubiquitin-dependent endocytosis of the IRON-REGULATED TRANSPORTER 1 (IRT1) transporter controls iron uptake in plants. Proceedings of the National Academy of Sciences. 2011; 108(32). doi: 10.1073/pnas.1100659108

Chen J, Zhao J, Yang S, et al. Prediction of Protein Ubiquitination Sites in Arabidopsis thaliana. Current Bioinformatics. 2019; 14(7): 614–620. doi: 10.2174/1574893614666190311141647




DOI: https://doi.org/10.18686/ppas.v5i1.1813

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