Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Plant Sci ; 339: 111949, 2024 Feb.
Article in English | MEDLINE | ID: mdl-38065304

ABSTRACT

5-Aminolevulinic acid (ALA), as a new natural plant growth regulator, has a significant function in promoting anthocyanin accumulation in many species of fruits. However, the mechanisms underlying remain obscure. In a transcriptome study of our group, it was found that many transcription factors (TFs) including NACs responsive to ALA treatment during anthocyanin accumulation. In the present study, we found a NAC of apple, MdNAC33 was coordinatively expressed with anthocyanin accumulation after ALA treatment in the apple fruits and leaves, suggesting that this TF may be involved in anthocyanin accumulation induced by ALA. We found that the MdNAC33 protein was localized in the nucleus and exhibited strong transcriptional activity in both yeast cells and plants, where its C-terminal contributed to the transcriptional activity. Functional analysis showed that overexpression of MdNAC33 promoted the accumulation of anthocyanin, while the silencing vector of MdNAC33 (RNAi) significantly impaired the anthocyanin accumulation induced by ALA. Yeast one-hybrid (Y1H), luciferase assay and electrophoretic mobility shift assay (EMSA) indicated that MdNAC33 could bind to promoters of MdbHLH3, MdDFR and MdANS to activate the gene expressions. In addition, MdNAC33 specifically interacts with MdMYB1, a positive regulator of anthocyanin biosynthesis, which was then in turn binding to its target genes MdUFGT and MdGSTF12, to promote anthocyanin accumulation in apples. Taken together, our data indicate that MdNAC33 plays multiple roles in ALA-induced anthocyanin biosynthesis. It provides new insights into the mechanisms of anthocyanin accumulation induced by ALA.


Subject(s)
Malus , Malus/genetics , Malus/metabolism , Transcription Factors/genetics , Transcription Factors/metabolism , Anthocyanins/metabolism , Saccharomyces cerevisiae/metabolism , Aminolevulinic Acid/metabolism , Plant Proteins/genetics , Plant Proteins/metabolism , Fruit/genetics , Fruit/metabolism , Gene Expression Regulation, Plant
2.
Biochim Biophys Acta ; 1797(11): 1795-806, 2010 Nov.
Article in English | MEDLINE | ID: mdl-20655869

ABSTRACT

BAX cooperates with truncated BID (tBID) and Ca(2+) in permeabilizing the outer mitochondrial membrane (OMM) and releasing mitochondrial apoptogenic proteins. The mechanisms of this cooperation are still unclear. Here we show that in isolated brain mitochondria, recombinant BAX readily self-integrates/oligomerizes in the OMM but produces only a minuscule release of cytochrome c, indicating that BAX insertion/oligomerization in the OMM does not always lead to massive OMM permeabilization. Ca(2+) in a mitochondrial permeability transition (mPT)-dependent and recombinant tBID in an mPT-independent manner promoted BAX insertion/ oligomerization in the OMM and augmented cytochrome c release. Neither tBID nor Ca(2+) induced BAX oligomerization in the solution without mitochondria, suggesting that BAX oligomerization required interaction with the organelles and followed rather than preceded BAX insertion in the OMM. Recombinant Bcl-xL failed to prevent BAX insertion/oligomerization in the OMM but strongly attenuated cytochrome c release. On the other hand, a reducing agent, dithiothreitol (DTT), inhibited BAX insertion/oligomerization augmented by tBID or Ca(2+) and suppressed the BAX-mediated release of cytochrome c and Smac/DIABLO but failed to inhibit Ca(2+)-induced swelling. Altogether, these data suggest that in brain mitochondria, BAX insertion/oligomerization can be dissociated from OMM permeabilization and that tBID and Ca(2+) stimulate BAX insertion/oligomerization and BAX-mediated OMM permeabilization by different mechanisms involving mPT induction and modulation of the SH-redox state.


Subject(s)
Brain/metabolism , Cell Membrane Permeability/physiology , Mitochondria/metabolism , Mitochondrial Membrane Transport Proteins/metabolism , Mitochondrial Membranes/metabolism , Sulfhydryl Compounds/pharmacology , bcl-2-Associated X Protein/metabolism , Animals , Apoptosis Regulatory Proteins , BH3 Interacting Domain Death Agonist Protein/metabolism , Calcium/metabolism , Carrier Proteins/metabolism , Humans , Male , Mice , Mitochondrial Permeability Transition Pore , Mitochondrial Proteins/metabolism , Mitochondrial Swelling , Oxidation-Reduction , Protein Multimerization , Rats , Rats, Sprague-Dawley , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , bcl-2-Associated X Protein/genetics , bcl-X Protein/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL
...