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1.
Plant Cell ; 27(4): 1061-81, 2015 Apr.
Article in English | MEDLINE | ID: mdl-25841037

ABSTRACT

Ethylene and abscisic acid (ABA) act synergistically or antagonistically to regulate plant growth and development. ABA is derived from the carotenoid biosynthesis pathway. Here, we analyzed the interplay among ethylene, carotenoid biogenesis, and ABA in rice (Oryza sativa) using the rice ethylene response mutant mhz5, which displays a reduced ethylene response in roots but an enhanced ethylene response in coleoptiles. We found that MHZ5 encodes a carotenoid isomerase and that the mutation in mhz5 blocks carotenoid biosynthesis, reduces ABA accumulation, and promotes ethylene production in etiolated seedlings. ABA can largely rescue the ethylene response of the mhz5 mutant. Ethylene induces MHZ5 expression, the production of neoxanthin, an ABA biosynthesis precursor, and ABA accumulation in roots. MHZ5 overexpression results in enhanced ethylene sensitivity in roots and reduced ethylene sensitivity in coleoptiles. Mutation or overexpression of MHZ5 also alters the expression of ethylene-responsive genes. Genetic studies revealed that the MHZ5-mediated ABA pathway acts downstream of ethylene signaling to inhibit root growth. The MHZ5-mediated ABA pathway likely acts upstream but negatively regulates ethylene signaling to control coleoptile growth. Our study reveals novel interactions among ethylene, carotenogenesis, and ABA and provides insight into improvements in agronomic traits and adaptive growth through the manipulation of these pathways in rice.


Subject(s)
Abscisic Acid/metabolism , Ethylenes/metabolism , Isomerases/metabolism , Oryza/metabolism , Plant Proteins/metabolism , Plant Roots/metabolism , Carotenoids/metabolism , Gene Expression Regulation, Plant
2.
Plant Physiol ; 163(2): 732-45, 2013 Oct.
Article in English | MEDLINE | ID: mdl-23940253

ABSTRACT

Excess light can have a negative impact on photosynthesis; thus, plants have evolved many different ways to adapt to different light conditions to both optimize energy use and avoid damage caused by excess light. Analysis of the Arabidopsis (Arabidopsis thaliana) mutant snowy cotyledon4 (sco4) revealed a mutation in a chloroplast-targeted protein that shares limited homology with CaaX-type endopeptidases. The SCO4 protein possesses an important function in photosynthesis and development, with point mutations rendering the seedlings and adult plants susceptible to photooxidative stress. The sco4 mutation impairs the acclimation of chloroplasts and their photosystems to excess light, evidenced in a reduction in photosystem I function, decreased linear electron transfer, yet increased nonphotochemical quenching. SCO4 is localized to the chloroplasts, which suggests the existence of an unreported type of protein modification within this organelle. Phylogenetic and yeast complementation analyses of SCO4-like proteins reveal that SCO4 is a member of an unknown group of higher plant-specific proteinases quite distinct from the well-described CaaX-type endopeptidases RAS Converting Enzyme1 (RCE1) and zinc metallopeptidase STE24 and lacks canonical CaaX activity. Therefore, we hypothesize that SCO4 is a novel endopeptidase required for critical protein modifications within chloroplasts, influencing the function of proteins involved in photosynthesis required for tolerance to excess light.


Subject(s)
Acclimatization/radiation effects , Arabidopsis Proteins/metabolism , Arabidopsis/enzymology , Arabidopsis/physiology , Light , Metalloendopeptidases/metabolism , Peptide Hydrolases/metabolism , Photosynthesis/radiation effects , Amino Acid Motifs , Arabidopsis/radiation effects , Chloroplasts/enzymology , Chloroplasts/radiation effects , Conserved Sequence , Ecotype , Electron Transport/radiation effects , Hydrogen Peroxide/metabolism , Mutation/genetics , Phenotype , Photobleaching/radiation effects , Photosystem I Protein Complex/metabolism , Photosystem II Protein Complex/metabolism , Phylogeny , Plant Leaves/physiology , Plant Leaves/radiation effects , Protein Transport/radiation effects , Seedlings/growth & development , Seedlings/radiation effects , Spectrometry, Fluorescence , Time Factors
3.
Plant Cell ; 23(11): 3992-4012, 2011 Nov.
Article in English | MEDLINE | ID: mdl-22128124

ABSTRACT

Compartmentation of the eukaryotic cell requires a complex set of subcellular messages, including multiple retrograde signals from the chloroplast and mitochondria to the nucleus, to regulate gene expression. Here, we propose that one such signal is a phosphonucleotide (3'-phosphoadenosine 5'-phosphate [PAP]), which accumulates in Arabidopsis thaliana in response to drought and high light (HL) stress and that the enzyme SAL1 regulates its levels by dephosphorylating PAP to AMP. SAL1 accumulates in chloroplasts and mitochondria but not in the cytosol. sal1 mutants accumulate 20-fold more PAP without a marked change in inositol phosphate levels, demonstrating that PAP is a primary in vivo substrate. Significantly, transgenic targeting of SAL1 to either the nucleus or chloroplast of sal1 mutants lowers the total PAP levels and expression of the HL-inducible ASCORBATE PEROXIDASE2 gene. This indicates that PAP must be able to move between cellular compartments. The mode of action for PAP could be inhibition of 5' to 3' exoribonucleases (XRNs), as SAL1 and the nuclear XRNs modulate the expression of a similar subset of HL and drought-inducible genes, sal1 mutants accumulate XRN substrates, and PAP can inhibit yeast (Saccharomyces cerevisiae) XRNs. We propose a SAL1-PAP retrograde pathway that can alter nuclear gene expression during HL and drought stress.


Subject(s)
Adenosine Diphosphate/metabolism , Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Chloroplasts/metabolism , Nucleotidases/metabolism , Arabidopsis/genetics , Arabidopsis Proteins/genetics , Ascorbate Peroxidases/genetics , Ascorbate Peroxidases/metabolism , Cell Nucleus/genetics , Droughts , Exoribonucleases/genetics , Exoribonucleases/metabolism , Gene Expression Regulation, Plant , Light , Mitochondria/metabolism , Mutation , Nucleotidases/genetics , Phosphoric Monoester Hydrolases , Plant Proteins/genetics , Plant Proteins/metabolism , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae Proteins/metabolism , Signal Transduction
4.
J Insect Physiol ; 57(2): 231-45, 2011 Feb.
Article in English | MEDLINE | ID: mdl-21078327

ABSTRACT

Gene silencing through RNA interference (RNAi) has revolutionized the study of gene function, particularly in non-model insects. However, in Lepidoptera (moths and butterflies) RNAi has many times proven to be difficult to achieve. Most of the negative results have been anecdotal and the positive experiments have not been collected in such a way that they are possible to analyze. In this review, we have collected detailed data from more than 150 experiments including all to date published and many unpublished experiments. Despite a large variation in the data, trends that are found are that RNAi is particularly successful in the family Saturniidae and in genes involved in immunity. On the contrary, gene expression in epidermal tissues seems to be most difficult to silence. In addition, gene silencing by feeding dsRNA requires high concentrations for success. Possible causes for the variability of success in RNAi experiments in Lepidoptera are discussed. The review also points to a need to further investigate the mechanism of RNAi in lepidopteran insects and its possible connection to the innate immune response. Our general understanding of RNAi in Lepidoptera will be further aided in the future as our public database at http://insectacentral.org/RNAi will continue to gather information on RNAi experiments.


Subject(s)
Gene Expression Regulation , Lepidoptera/genetics , Lepidoptera/immunology , RNA Interference , Animals , Databases, Genetic , Epidermis/growth & development , Gene Silencing , Immunity, Innate , Insect Proteins/drug effects , Insect Proteins/genetics , Insect Proteins/immunology , Lepidoptera/drug effects , Lepidoptera/growth & development , RNA, Double-Stranded/drug effects , Research Design
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