Antagonistic actions of Arabidopsis cryptochromes and phytochrome B in the regulation of floral induction.
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The Arabidopsis photoreceptors cry1, cry2 and phyB are known to play roles in the regulation of flowering time, for which the molecular mechanisms remain unclear. We have previously hypothesized that phyB mediates a red-light inhibition of floral initiation and cry2 mediates a blue-light inhibition of the phyB function. Studies of the cry2/phyB double mutant provide direct evidence in support of this hypothesis. The function of cryptochromes in floral induction was further investigated using the cry2/cry1 double mutants. The cry2/cry1 double mutants showed delayed flowering in monochromatic blue light, whereas neither monogenic cry1 nor cry2 mutant exhibited late flowering in blue light. This result suggests that, in addition to the phyB-dependent function, cry2 also acts redundantly with cry1 to promote floral initiation in a phyB-independent manner. To understand how photoreceptors regulate the transition from vegetative growth to reproductive development, we examined the effect of sequential illumination by blue light and red light on the flowering time of plants. We found that there was a light-quality-sensitive phase of plant development, during which the quality of light exerts a profound influence on flowering time. After this developmental stage, which is between approximately day-1 to day-7 post germination, plants are committed to floral initiation and the quality of light has little effect on the flowering time. Mutations in either the PHYB gene or both the CRY1 and CRY2 genes resulted in the loss of the light-quality-sensitive phase manifested during floral development. The commitment time of floral transition, defined by a plant's sensitivity to light quality, coincides with the commitment time of inflorescence development revealed previously by a plant's sensitivity to light quantity - the photoperiod. Therefore, the developmental mechanism resulting in the commitment to flowering appears to be the direct target of the antagonistic actions of the photoreceptors. (+info)
A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.
(66/18423)
Arabidopsis thaliana BAC T07M07 encoding the abscisic acid-insensitive 4 (ABI4) locus has been sequenced completely. It contains a 95,713-bp insert and 24 predicted genes. Most putative genes were confirmed by gel-based RNA profiling and a cluster of ABA-regulated genes was identified. One of the 24 genes, designated PP2C5, encodes a putative protein phosphatase 2C. The encoded protein was expressed in Escherichia coli, and its enzyme activity in vitro was confirmed. (+info)
Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth.
(67/18423)
Pollen tube cells elongate based on actin- dependent targeted secretion at the tip. Rho family small GTPases have been implicated in the regulation of related processes in animal and yeast cells. We have functionally characterized Rac type Rho family proteins that are expressed in growing pollen tubes. Expression of dominant negative Rac inhibited pollen tube elongation, whereas expression of constitutive active Rac induced depolarized growth. Pollen tube Rac was found to accumulate at the tip plasma membrane and to physically associate with a phosphatidylinositol monophosphate kinase (PtdIns P-K) activity. Phosphatidylinositol 4, 5-bisphosphate (PtdIns 4, 5-P2), the product of PtdIns P-Ks, showed a similar intracellular localization as Rac. Expression of the pleckstrin homology (PH)-domain of phospholipase C (PLC)-delta1, which binds specifically to PtdIns 4, 5-P2, inhibited pollen tube elongation. These results indicate that Rac and PtdIns 4, 5-P2 act in a common pathway to control polar pollen tube growth and provide direct evidence for a function of PtdIns 4, 5-P2 compartmentalization in the regulation of this process. (+info)
Photomophogenesis: Phytochrome takes a partner!
(68/18423)
How light signals are transduced by phytochromes is still poorly understood. Recent studies have provided evidence that a PAS domain protein, PIF3, physically interacts with phytochromes, plays a role in phytochrome signal transduction and might be a component of a novel signalling pathway in plants. (+info)
Circadian rhythms: Something to cry about?
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Recent studies suggest that a class of proteins known as cryptochromes have an evolutionarily conserved role in the entrainment of circadian rhythms to the night-day cycle. While the evidence reported is intriguing, the notion that cryptochromes have the same role in all species requires further investigation. (+info)
A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes.
(70/18423)
Short-chain acyl-CoA oxidases are beta-oxidation enzymes that are active on short-chain acyl-CoAs and that appear to be present in higher plant peroxisomes and absent in mammalian peroxisomes. Therefore, plant peroxisomes are capable of performing complete beta-oxidation of acyl-CoA chains, whereas mammalian peroxisomes can perform beta-oxidation of only those acyl-CoA chains that are larger than octanoyl-CoA (C8). In this report, we have shown that a novel acyl-CoA oxidase can oxidize short-chain acyl-CoA in plant peroxisomes. A peroxisomal short-chain acyl-CoA oxidase from Arabidopsis was purified following the expression of the Arabidopsis cDNA in a baculovirus expression system. The purified enzyme was active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Cell fractionation and immunocytochemical analysis revealed that the short-chain acyl-CoA oxidase is localized in peroxisomes. The expression pattern of the short-chain acyl-CoA oxidase was similar to that of peroxisomal 3-ketoacyl-CoA thiolase, a marker enzyme of fatty acid beta-oxidation, during post-germinative growth. Although the molecular structure and amino acid sequence of the enzyme are similar to those of mammalian mitochondrial acyl-CoA dehydrogenase, the purified enzyme has no activity as acyl-CoA dehydrogenase. These results indicate that the short-chain acyl-CoA oxidases function in fatty acid beta-oxidation in plant peroxisomes, and that by the cooperative action of long- and short-chain acyl-CoA oxidases, plant peroxisomes are capable of performing the complete beta-oxidation of acyl-CoA. (+info)
Systemic signaling and acclimation in response to excess excitation energy in Arabidopsis.
(71/18423)
Land plants are sessile and have developed sophisticated mechanisms that allow for both immediate and acclimatory responses to changing environments. Partial exposure of low light-adapted Arabidopsis plants to excess light results in a systemic acclimation to excess excitation energy and consequent photooxidative stress in unexposed leaves. Thus, plants possess a mechanism to communicate excess excitation energy systemically, allowing them to mount a defense against further episodes of such stress. Systemic redox changes in the proximity of photosystem II, hydrogen peroxide, and the induction of antioxidant defenses are key determinants of this mechanism of systemic acquired acclimation. (+info)
A leucine-rich repeat protein of carrot that exhibits antifreeze activity.
(72/18423)
A gene encoding an antifreeze protein (AFP) was isolated from carrot (Daucus carota) using sequence information derived from the purified protein. The carrot AFP is highly similar to the polygalacturonase inhibitor protein (PGIP) family of apoplastic plant leucine-rich repeat (LRR) proteins. Expression of the AFP gene is rapidly induced by low temperatures. Furthermore, expression of the AFP gene in transgenic Arabidopsis thaliana plants leads to an accumulation of antifreeze activity. Our findings suggest that a new type of plant antifreeze protein has recently evolved from PGIPs. (+info)