Phytochromes are a class of photoreceptor in plants, bacteria and fungi used to detect light. They are sensitive to light in the red and far-red region of the visible spectrum and can be classed as either Type I, which are activated by far-red light, or Type II that are activated by red light. Recent advances have suggested that phytochromes also act as temperature sensors, as warmer temperatures enhance their de-activation. All of these factors contribute to the plant's ability to germinate.
Phytochromes control many aspects of plant development. They regulate the germination of seeds (photoblasty), the synthesis of chlorophyll, the elongation of seedlings, the size, shape and number and movement of leaves and the timing of flowering in adult plants. Phytochromes are widely expressed across many tissues and developmental stages.
Other plant photoreceptors include cryptochromes and phototropins, which respond to blue and ultraviolet-A light and UVR8, which is sensitive to ultraviolet-B light.
In addition to their roles in nature, the light-induced interaction between a plant phytochrome and phytochrome-interacting factor (PIF) was used in 2002 to control gene transcription in yeast. This was the first example of using photoproteins from another organism for controlling a biochemical pathway.
Phytochromes consist of a protein, covalently linked to a light-sensing bilin chromophore. The protein part comprises two identical chains (A and B). Each chain has a PAS domain, GAF domain and PHY domain. Domain arrangements in plant, bacterial and fungal phytochromes are comparable, insofar as the three N-terminal domains are always PAS, GAF and PHY domains. However C-terminal domains are more divergent. The PAS domain serves as a signal sensor and the GAF domain is responsible for binding to cGMP and also senses light signals. Together, these subunits form the phytochrome region, which regulates physiological changes in plants to changes in red and far red light conditions.
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Photoperiodism is the physiological reaction of organisms to the length of night or a dark period. It occurs in plants and animals. Plant photoperiodism can also be defined as the developmental responses of plants to the relative lengths of light and dark periods. They are classified under three groups according to the photoperiods: short-day plants, long-day plants, and day-neutral plants. Many flowering plants (angiosperms) use a photoreceptor protein, such as phytochrome or cryptochrome, to sense seasonal changes in night length, or photoperiod, which they take as signals to flower.
Cryptochromes (from the Greek κρυπτός χρώμα, "hidden colour") are a class of flavoproteins found in plants and animals that are sensitive to blue light. They are involved in the circadian rhythms and the sensing of magnetic fields in a number of species. The name cryptochrome was proposed as a portmanteau combining the chromatic nature of the photoreceptor, and the cryptogamic organisms on which many blue-light studies were carried out. The genes Cry1 and Cry2 encode the two cryptochrome proteins CRY1 and CRY2, respectively.
Maize (meɪz ; Zea mays subsp. mays, from maíz after mahis), also known as corn in North American- and Australian- English, is a cereal grain first domesticated by indigenous peoples in southern Mexico about 10,000 years ago. The leafy stalk of the plant gives rise to inflorescences (or "tassels") which produce pollen and separate ovuliferous inflorescences called ears that when fertilized yield kernels or seeds, which are botanical fruits.
TiO2 quantum dot (QD) size nanoparticle colloids have shown tremendous photochromic response. Here we show that the of the photochromic response of TiO2 QDs can be further enhanced by doping. Our synthesis approach allows to reach high nominal doping level ...
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The plant ultraviolet-B (UV-B) photoreceptor UVR8 plays an important role in UV-B acclimation and survival. UV-B absorption by homodimeric UVR8 induces its monomerization and interaction with the E3 ubiquitin ligase COP1, leading ultimately to gene express ...
Endoplasmic reticulum (ER) retention of misfolded glycoproteins is mediated by the ER-localized eukaryotic glycoprotein secretion checkpoint, UDP-glucose glycoprotein glucosyl-transferase (UGGT). The enzyme recognizes a misfolded glycoprotein and flags it ...