Reactive Byproducts of Plant Redox Metabolism and Protein Functions.

Acta Naturae

St Petersburg University, St. Petersburg, 199034 Russian Federation.

Published: January 2024

Living organisms exhibit an impressive ability to expand the basic information encoded in their genome, specifically regarding the structure and function of protein. Two basic strategies are employed to increase protein diversity and functionality: alternative mRNA splicing and post-translational protein modifications (PTMs). Enzymatic regulation is responsible for the majority of the chemical reactions occurring within living cells. However, plants redox metabolism perpetually generates reactive byproducts that spontaneously interact with and modify biomolecules, including proteins. Reactive carbonyls resulted from the oxidative metabolism of carbohydrates and lipids carbonylate proteins, leading to the latter inactivation and deposition in the form of glycation and lipoxidation end products. The protein nitrosylation caused by reactive nitrogen species plays a crucial role in plant morphogenesis and stress reactions. The redox state of protein thiol groups modified by reactive oxygen species is regulated through the interplay of thioredoxins and glutaredoxins, thereby influencing processes such as protein folding, enzyme activity, and calcium and hormone signaling. This review provides a summary of the PTMs caused by chemically active metabolites and explores their functional consequences in plant proteins.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11771839PMC
http://dx.doi.org/10.32607/actanaturae.27477DOI Listing

Publication Analysis

Top Keywords

reactive byproducts
8
redox metabolism
8
protein
7
reactive
5
byproducts plant
4
plant redox
4
metabolism protein
4
protein functions
4
functions living
4
living organisms
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!