Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

The study focuses on the uptake, accumulation, and translocation of polycyclic aromatic hydrocarbons (PAHs) in cereals, specifically exploring the role of peroxidase (UniProt accession: A0A3B5XXD0, abbreviation: PX1) and unidentified protein (UniProt accession: A0A3B6LUC6, abbreviation: UP1) in phenanthrene solubilization within wheat xylem sap. This research aims to clarify the interactions between these proteins and phenanthrene. Employing both in vitro and in vivo analyses, we evaluated the solubilization capabilities of recombinant transport proteins for phenanthrene and examined the relationship between protein expression and phenanthrene concentration. UP1 displayed greater transport efficiency, while PX1 excelled at lower concentrations. Elevated PX1 levels contributed to phenanthrene degradation, marginally diminishing its transport. Spectral analyses and molecular dynamics simulations validated the formation of stable protein-phenanthrene complexes. The study offers crucial insights into PAH-related health risks in crops by elucidating the mechanisms of PAH accumulation facilitated by transport proteins. Copyright © 2023 Elsevier Masson SAS. All rights reserved.

Citation

Nengde Zeng, Chenghao Huang, Fei Huang, Jiani Du, Dongru Wang, Xinhua Zhan, Baoshan Xing. Transport proteins and their differential roles in the accumulation of phenanthrene in wheat. Plant physiology and biochemistry : PPB. 2024 Jan;206:108275

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 38103340

View Full Text