Regulation of Cadmium-Induced Proteomic and Metabolic Changes by 5-Aminolevulinic Acid in Leaves of Brassica napus L.
Author(s) -
Basharat Ali,
Rafaqat A. Gill,
Su Yang,
Muhammad Bilal Gill,
Muhammad Ahsan Farooq,
Dan Liu,
Muhammad Daud,
Shafaqat Ali,
Weijun Zhou
Publication year - 2015
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0123328
Subject(s) - biochemistry , proteasome , biology , dihydrolipoamide dehydrogenase , proteomics , protein subunit , brassica , protochlorophyllide , ribosomal protein , chemistry , microbiology and biotechnology , enzyme , dehydrogenase , botany , gene , biosynthesis , ribosome , rna
It is evident from previous reports that 5-aminolevulinic acid (ALA), like other known plant growth regulators, is effective in countering the injurious effects of heavy metal-stress in oilseed rape ( Brassica napus L.). The present study was carried out to explore the capability of ALA to improve cadmium (Cd 2+ ) tolerance in B . napus through physiological, molecular, and proteomic analytical approaches. Results showed that application of ALA helped the plants to adjust Cd 2+ -induced metabolic and photosynthetic fluorescence changes in the leaves of B . napus under Cd 2+ stress. The data revealed that ALA treatment enhanced the gene expressions of antioxidant enzyme activities substantially and could increase the expression to a certain degree under Cd 2+ stress conditions. In the present study, 34 protein spots were identified that differentially regulated due to Cd 2+ and/or ALA treatments. Among them, 18 proteins were significantly regulated by ALA, including the proteins associated with stress related, carbohydrate metabolism, catalysis, dehydration of damaged protein, CO2 assimilation/photosynthesis and protein synthesis/regulation. From these 18 ALA-regulated proteins, 12 proteins were significantly down-regulated and 6 proteins were up-regulated. Interestingly, it was observed that ALA-induced the up-regulation of dihydrolipoyl dehydrogenase, light harvesting complex photo-system II subunit 6 and 30S ribosomal proteins in the presence of Cd 2+ stress. In addition, it was also observed that ALA-induced the down-regulation in thioredoxin-like protein, 2, 3-bisphosphoglycerate, proteasome and thiamine thiazole synthase proteins under Cd 2+ stress. Taken together, the present study sheds light on molecular mechanisms involved in ALA-induced Cd 2+ tolerance in B . napus leaves and suggests a more active involvement of ALA in plant physiological processes than previously proposed.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom