ANTHOCYANIN production is primarily controlled by the Cryptochrome (CR1) Photoreceptor ( !! UV and Blue Spectrums are primary drivers in the production of the pigment that replaces chlorophyll, isn't that awesome! 1. Diverse photoreceptors in plants Many civilizations, including the sun god of ancient Egypt, thought that the blessings of sunlight were the source of life. In fact, the survival of all life, including humans, is supported by the photosynthesis of plants that capture solar energy. Plants that perform photosynthesis have no means of transportation except for some algae. Therefore, it is necessary to monitor various changes in the external environment and respond appropriately to the place to survive. Among various environmental information, light is especially important information for plants that perform photosynthesis. In the process of evolution, plants acquired phytochrome, which mainly receives light in the red light region, and multiple blue light receptors, including his hytropin and phototropin, in order to sense the light environment. .. In addition to these, an ultraviolet light receptor named UVR8 was recently discovered. The latest image of the molecular structure and function of these various plant photoreceptors (Fig. 1), focusing on phytochrome and phototropin. Figure 1 Ultraviolet-visible absorption spectra of phytochrome, cryptochrome, phototropin, and UVR8. The dashed line represents each bioactive absorption spectrum. 2. Phytochrome; red-far red photoreversible molecular switch What is phytochrome? Phytochrome is a photochromic photoreceptor, and has two absorption types, a red light absorption type Pr (absorption maximum wavelength of about 665 nm) and a far-red light absorption type Pfr (730 nm). Reversible light conversion between the two by red light and far-red light, respectively(Fig. 1A, solid line and broken line). In general, Pfr is the active form that causes a physiological response. With some exceptions, phytochrome can be said to function as a photoreversible molecular switch. The background of the discovery is as follows. There are some types of plants that require light for germination (light seed germination). From that study, it was found that germination was induced by red light, the effect was inhibited by subsequent far-red light irradiation, and this could be repeated, and the existence of photoreceptors that reversibly photoconvert was predicted. In 1959, its existence was confirmed by the absorption spectrum measurement of the yellow sprout tissue, and it was named phytochrome. Why does the plant have a sensor to distinguish between such red light and far-red light? There is no big difference between the red and far-red light regions in the open-field spectrum of sunlight, but the proportion of red light is greatly reduced due to the absorption of chloroplasts in the shade of plants. Similar changes in light quality occur in the evening sunlight. Plants perceive this difference in light quality as the ratio of Pr and Pfr, recognize the light environment, and respond to it. Subsequent studies have revealed that it is responsible for various photomorphogenic reactions such as photoperiodic flowering induction, shade repellent, and deyellowing (greening). Furthermore, with the introduction of the model plant Arabidopsis thaliana (At) and the development of molecular biological analysis methods, research has progressed dramatically, and his five types of phytochromes (phyA-E) are present in Arabidopsis thaliana. all right. With the progress of the genome project, Fi’s tochrome-like photoreceptors were found in cyanobacteria, a photosynthetic prokaryotes other than plants. Furthermore, in non-photosynthetic bacteria, a homologue molecule called bacteriophytochrome photoreceptor (BphP) was found in Pseudomonas aeruginosa (Pa) and radiation-resistant bacteria (Deinococcus radiodurans, Dr). Domain structure of phytochrome molecule Phytochrome molecule can be roughly divided into N-terminal side and C-terminal side region. PAS (Per / Arndt / Sim: blue), GAF (cGMP phosphodiesterase / adenylyl cyclase / FhlA: green), PHY (phyto-chrome: purple) 3 in the N-terminal region of plant phytochrome (Fig. 2A) There are two domains and an N-terminal extension region (NTE: dark blue), and phytochromobilin (PΦB), which is one of the ring-opening tetrapyrroles, is thioether-bonded to the system stored in GAF as a chromophore. ing. PAS is a domain involved in the interaction between signal transduction-related proteins, and PHY is a phytochrome-specific domain. There are two PASs and her histidine kinase-related (HKR) domain (red) in the C-terminal region, but the histidine essential for kinase activity is not conserved. 3. Phototropin; photosynthetic efficiency optimized blue light receptor What is phototropin? Charles Darwin, who is famous for his theory of evolution, wrote in his book “The power of move-ment in plants” published in 1882 that plants bend toward blue light. Approximately 100 years later, the protein nph1 (nonphoto-tropic hypocotyl 1) encoded by one of the causative genes of Arabidopsis mutants causing phototropic abnormalities was identified as a blue photoreceptor. Later, another isotype npl1 was found and renamed phototropin 1 (phot1) and 2 (phot2), respectively. In addition to phototropism, phototropin is damaged by chloroplast photolocalization (chloroplasts move through the epidermal cells of the leaves and gather on the cell surface under appropriate light intensity for photosynthesis. As a photoreceptor for reactions such as escaping to the side of cells under dangerous strong light) and stomata (reactions that open stomata to optimize the uptake of carbon dioxide, which is the rate-determining process of photosynthetic reactions). It became clear that it worked. In this way, phototropin can be said to be a blue light receptor responsible for optimizing photosynthetic efficiency. Domain structure and LOV photoreaction of phototropin molecule Phototropin molecule has two photoreceptive domains (LOV1 and LOV2) called LOV (Light-Oxygen-Voltage sensing) on the N-terminal side, and serine / on the C-terminal side. It is a protein kinase that forms threonine kinase (STK) (Fig. 4Aa) and whose activity is regulated by light. LOV is one molecule as a chromophore, he binds FMN (flavin mononucleotide) non-covalently. The LOV forms an α/βfold, and the FMN is located on a β-sheet consisting of five antiparallel β-strands (Fig. 4B). The FMN in the ground state LOV shows the absorption spectrum of a typical oxidized flavin protein with a triplet oscillation structure and an absorption maximum wavelength of 450 nm, and is called D450 (Fig. 1C and Fig. 4E). After being excited to the singlet excited state by blue light, the FMN shifts to the triplet excited state (L660t *) due to intersystem crossing, and then the C4 (Fig. 4C) of the isoaroxazine ring of the FMN is conserved in the vicinity. It forms a transient accretionary prism with the tain (red part in Fig. 4B Eα) (S390I). When this cysteine is replaced with alanine (C / A substitution), the addition reaction does not occur. The effect of adduct formation propagates to the protein moiety, causing kinase activation (S390II). After that, the formed cysteine-flavin adduct spontaneously dissociates and returns to the original D450 (Fig. 4E, dark regression reaction). Phototropin kinase activity control mechanism by LOV2 Why does phototropin have two LOVs? Atphot1 was found as a protein that is rapidly autophosphorylated when irradiated with blue light. The effect of the above C / A substitution on this self-phosphorylation reaction and phototropism was investigated, and LOV2 is the main photomolecular switch in both self-phosphorylation and phototropism. It turns out that it functions as. After that, from experiments using artificial substrates, STK has a constitutive activity, LOV2 functions as an inhibitory domain of this activity, and the inhibition is eliminated by photoreaction, while LOV1 is kinase light. It was shown to modify the photosensitivity of the activation reaction. In addition to this, LOV1 was found to act as a dimerization site from the crystal structure and his SAXS. What kind of molecular mechanism does LOV2 use to photoregulate kinase activity? The following two modules play important roles in this intramolecular signal transduction. Figure 4 (A) Domain structure of LOV photoreceptors. a: Phototropin b: Neochrome c: FKF1 family protein d: Aureochrome (B) Crystal structure of auto barley phot1 LOV2. (C) Structure of FMN isoaroxazine ring. (D) Schematic diagram of the functional domain and module of Arabidopsis thaliana phot1. L, A’α, and Jα represent linker, A’α helix, and Jα helix, respectively. (E) LOV photoreaction. (F) Molecular structure model (mesh) of the LOV2-STK sample (black line) containing A’α of phot2 obtained based on SAXS under dark (top) and under bright (bottom). The yellow, red, and green space-filled models represent the crystal structures of LOV2-Jα, protein kinase A N-lobe, and C-robe, respectively, and black represents FMN. See the text for details. 1) Jα. LOV2 C of oat phot1-to α immediately after the terminus Rix (Jα) is present (Fig. 4D), which interacts with the β-sheet (Fig. 4B) that forms the FMN-bound scaffold of LOV2 in the dark, but unfolds and dissociates from the β-sheet with photoreaction. It was shown by NMR that it does. According to the crystal structure of LOV2-Jα, this Jα is located on the back surface of the β sheet and mainly has a hydrophobic interaction. The formation of S390II causes twisting of the isoaroxazine ring and protonation of N5 (Fig. 4C). As a result, the glutamine side chain present on his Iβ strand (Fig. 4B) in the β-sheet rotates to form a hydrogen bond with this protonated N5. Jα interacts with this his Iβ strand, and these changes are thought to cause the unfold-ing of Jα and dissociation from the β-sheet described above. Experiments such as amino acid substitution of Iβ strands revealed that kinases exhibit constitutive activity when this interaction is eliminated, and that Jα plays an important role in photoactivation of kinases. 2) A’α / Aβ gap. Recently, several results have been reported showing the involvement of amino acids near the A’α helix (Fig. 4D) located upstream of the N-terminal of LOV2 in kinase photoactivation. Therefore, he investigated the role of this A’α and its neighboring amino acids in kinase photoactivation, photoreaction, and Jα structural change for Atphot1. The LOV2-STK polypeptide (Fig. 4D, underlined in black) was used as a photocontrollable kinase for kinase activity analysis. As a result, it was found that the photoactivation of the kinase was abolished when amino acid substitution was introduced into the A’α / Aβ gap between A’α and Aβ of the LOV2 core. Interestingly, he had no effect on the structural changes in Jα examined on the peptide map due to the photoreaction of LOV2 or trypsin degradation. Therefore, the A’α / Aβ gap is considered to play an important role in intramolecular signal transduction after Jα. Structural changes detected by SAXS Structural changes of Jα have been detected by various biophysical methods other than NMR, but structural information on samples including up to STK is reported only by his results to his SAXS. Not. The SAXS measurement of the Atphot2 LOV2-STK polypeptide showed that the radius of inertia increased from 32.4 Å to 34.8 Å, and the molecular model (Fig. 4F) obtained by the ab initio modeling software GASBOR is that of LOV2 and STK. It was shown that the N lobes and C lobes lined up in tandem, and the relative position of LOV2 with respect to STK shifted by about 13 Å under light irradiation. The difference in the molecular model between the two is considered to reflect the structural changes that occur in the Jα and A’α / Aβ gaps mentioned above. Two phototropins with different photosensitivity In the phototropic reaction of Arabidopsis Arabidopsis, Arabidopsis responds to a very wide range of light intensities from 10–4 to 102 μmol photon / sec / m2. At that time, phot1 functions as an optical sensor in a wide range from low light to strong light, while phot2 reacts with light stronger than 1 μmol photon / sec / m2. What is the origin of these differences? As is well known, animal photoreceptors have a high photosensitivity due to the abundance of rhodopsin and the presence of biochemical amplification mechanisms. The exact abundance of phot1 and phot2 in vivo is unknown, but interesting results have been obtained in terms of amplification. The light intensity dependence of the photoactivation of the LOV2-STK polypeptide used in the above kinase analysis was investigated. It was found that phot1 was about 10 times more photosensitive than phot2. On the other hand, when the photochemical reactions of both were examined, it was found that the rate of the dark return reaction of phot1 was about 10 times slower than that of phot2. This result indicates that the longer the lifetime of S390II, which is in the kinase-activated state, the higher the photosensitivity of kinase activation. This correlation was further confirmed by extending the lifespan of her S390II with amino acid substitutions. This alone cannot explain the widespread differences in photosensitivity between phot1 and phot2, but it may explain some of them. Furthermore, it is necessary to investigate in detail protein modifications such as phosphorylation and the effects of phot interacting factors on photosensitivity. Other LOV photoreceptors Among fern plants and green algae, phytochrome ɾphotosensory module (PSM) on the N-terminal side and chimera photoreceptor with full-length phototropin on the C-terminal side, neochrome (Fig. There are types with 4Ab). It has been reported that some neochromes play a role in chloroplast photolocalization as a red light receiver. It is considered that fern plants have such a chimera photoreceptor in order to survive in a habitat such as undergrowth in a jungle where only red light reaches. In addition to this, plants have only one LOV domain, and three proteins involved in the degradation of photomorphogenesis-related proteins, FKF1 (Flavin-binding, Kelch repeat, F-box 1, ZTL (ZEITLUPE)), LKP2 ( There are LOV Kelch Protein2) (Fig. 4Ac) and aureochrome (Fig. 4Ad), which has a bZip domain on the N-terminal side of LOV and functions as a gene transcription factor. 4. Cryptochrome and UVR8 Cryptochrome is one of the blue photoreceptors and forms a superfamily with the DNA photoreceptor photolyase. It has FAD (flavin adenine dinucle-otide) as a chromophore and tetrahydrofolic acid, which is a condensing pigment. The ground state of FAD is considered to be the oxidized type, and the radical type (broken line in Fig. 1B) generated by blue light irradiation is considered to be the signaling state. The radical type also absorbs in the green to orange light region, and may widen the wavelength region of the plant morphogenesis reaction spectrum. Cryptochrome uses blue light to control physiological functions similar to phytochrome. It was identified as a photoreceptor from one of the causative genes of UVR8 Arabidopsis thaliana, and the chromophore is absorbed in the UVB region by a Trp triad consisting of three tryptophans (Fig. 1D). It is involved in the biosynthesis of flavonoids and anthocyanins that function as UV scavengers in plants. Conclusion It is thought that plants have acquired various photoreceptors necessary for their survival during a long evolutionary process. The photoreceptors that cover the existing far-red light to UVB mentioned here are considered to be some of them. More and more diverse photoreceptor genes are conserved in cyanobacteria and marine plankton. By examining these, it is thought that the understanding of plant photoreceptors will be further deepened.

2/28: Fed today...last dose of nutes. 3/3: Gave her plain water and liquidsoil today..will flush her soon.

Hey everyone 😃. Day 1 : The seeds were placed between 2 moist towels to germinate and sealed in a box. Day 2 : No change . Day 3: Both seeds have sprouted and you can see a small tip of the root coming out. Day 4: The tip of the root looks out about 0.5 - 1 cm. today they were set in stone wool blocks. These were placed in water beforehand and mixed with a little Rizotonic to stimulate root formation. Day 5: Today, both seedlings stick their heads out about 1 cm 😊. (The grow box is sprayed under the hood every day to keep it moist.) Day 6: Today the heads are already looking 2 cm out. Day 7: Both rock wool blocks were planted in Canna Coco, and some water with an Ec mixture 0.4 was added. So they stay under the hood for about 7-10 days. (The lid is opened a little wider every 2-3 days to get used to the lower humidity. I hope you have a lot of fun with the update, stay healthy and let it grow 🙏🏻😊 You can buy this Strain at : https://www.royalqueenseeds.de/feminisierte-hanfsamen/115-amnesia-haze.html Type: Amnesia Haze ☝️🏼 Genetics: Original Amnesia Haze 👍 Vega lamp: 2 x Todogrow Led Quantum Board 100 W 💡 Bloom Lamp : 2 x Todogrow Led Cxb 3590 COB 3500 K 205W 💡💡☝️🏼 Soil : Canna Coco Professional + ☝️🏼 Fertilizer: Green House Powder Feeding ☝️🏼🌱 Water: Osmosis water mixed with normal water (24 hours stale that the chlorine evaporates) to 0.2 EC. Add Cal / Mag to 0.4 Ec Ph with Organic Ph - to 5.5 - 5.8 .

Welcome to veg Week 4 of Sweet Seeds Mental Rainbow F1 I'm excited to share my grow journey with you from my Sweet Seeds Project . It's going to be an incredible ride, full of learning, growing, and connecting with fellow growers from all around the world! For this Project , I’ve chosen the Feminized Photo strain Mental Rainbow F1 : Here’s what I’m working with: • 🌱 Tent: 120x60x80 • 🧑‍🌾 Breeder Company: Sweet Seeds • 💧 Humidity Range: 60 • ⏳ Flowering Time: 7-8weeks • Strain Info: 22-30%THC • 🌡️ Temperature: 26 • 🍵 Pot Size: 0.5l • Nutrient Brand: Narcos • ⚡ Lights : 600W x 2 A huge thank you to Sweet Seeds for allowing me to try my Best with this amazing collection from Photo Strains they managed to Sponsore . Big thanks for supporting the grower community worldwide! Your genetics and passion speak for themselves! I would truly appreciate every bit of feedback, help, questions, or discussions – and of course, your likes and interactions mean the world to me as I try to stand out in this exciting competition! Let’s grow together – and don’t forget to stop by again to see the latest updates! Happy growing! Stay lifted and stay curious! Peace & Buds!

Plant starts off slower than others. But once she’s in flower and starts packing on resin and changing colors, everything changes. The plant reeks of funky terps and citrus and just stinky goodness. The colors are crazy ranging from pink to blue and purple. Highly recommend this strain and she produces super fat sticky buds. She’s a keeper.

Day 85. Just before lights photo's for better true colour understanding, Bio Grow and AlgaMic is out, after finishing this cycle CalMag and Silica out too. Hope its not too early, but girls are really healthy, time to pump up the flowers not leaves :) Day 86. Girls just flying, very happy with Gorillas and Control Garden looks really funky, they stand under no direct light on them... and still flowers looks amazing. Got my new mobile, had to try out :) Next week very busy at work, no updates I think. Day 89. So again i made mistake, while watering them last time accidently left heater on, they overdried , plus temps where at +33c ... Bunny Gorilla looks bad, Gorilla Max got biggest pistil damage, half went brown. Thinking i took nitrogen too early out, but we shall see. On other hand all Control Garden took it well even Cookies with theirs waxy leaves stood thurst nice as such stress can be ... Planing to do defoliation next week, but if Gorillas started to eat themselves already will leave them as it is. Future will show .. Happy Growing !!!

Day 39 she’s huge very very happy with the way she is turning out. She’s exploded and very large and in charge. I’m stoked on her.

Week 7 begins for Mandarin dreams. Both ladies are looking good and healthy, bud sites continue to bulk up and frost up. The shirt smell from MD1 has gone away, it's current smell is a bit earthy. Switched out big bud coco for overdrive as we approach the end of the grow. Thanks for checking in, tune in next week! 👽🌳🔥

Sooo I forgot to update the diary for about 3 weeks,good thing is you guys didnt miss that much cause I got the luck to have a more sativa pheno, thats why this girl will prob still take another good 3-4 weeks. Shes getting fatter every day, the calyx started turning purple around the plant so maybe just a classic „cookies“ pheno or maybe even a whole purple plant who knows what will happen with her when we start to flush.

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Buds looking alright. Leaves have seen better days & I feel like she's dying on me... Swapped the light because my friend who 'claims he's an expert' told me too. Flushed 20th will go for a 2-week flush even with this flawless finish. (if they make it that long) My tap water is 360ppm & runoff is 415 after flush (30+L of PH'd water) I am definitely going to do a 48-hour dark period before harvest with no watering. Anything I'm doing wrong let me know!

04/10 la belle se lève et s'élève

We had storms. Plants nearly survived. I gave them support. Now they seem fine but the leaves weight is to big for the stem.🙃 Lots of attitude for a two week old.

Día 9 (10/06) N/A Día 10 (11/06) N/A Día 11 (12/06) Llueve mucho. Humedad alta por aquí. Eso les favorece Día 12 (13/06) Se empiezan a desarrollar las hojas verdaderas a una buena velocidad! Todo en marcha! 💨 Día 13 (14/06) Riego ligero 100 ml sólo H20 EC 0,5 en previsión del trasplante en el día 15 de la planta Día 14 (15/06) Se nota que estamos en el día 14 desde germinación y la mayoría de las plántulas van viento en popa! Día 15 (16/06) Hoy procedemos a trasplantar a las chicas a su maceta intermedia de 6,5 litros Se prepara con 5,5 Litros (85%) de sustrato PRO-MIX HP BACILLUS+MYCORRHIZAE + 1 Litro de Insect Frass (15%) + 65 gramos de Earth Vibes Super Soil (10 g/L substrato) Se llena la maceta de sustrato con las manos (limpias) y rompiendo los trozos más gruesos, para que el sustrato esté aireado y esponjoso, sin presionar Se coloca una maceta vacía de 1L para que quede la forma perfecta de la maceta donde están las plántulas (ver fotos) Se espolvorea la parte proporcional de la probeta de microorganismos sobre el agujero de trasplante Se saca la plántula de su maceta actual (bonitas raíces 😍) y se coloca en la maceta final Se riega muy lentamente hasta percolación profunda con H2O EC 0,5 pH 6,5 Se coloca mulch (acolchado) de paja para evitar traspiración excesiva y cuidar a los microorganismos del suelo A ver como reacciona al trasplante! 💦Nutrients by Lurpe Solutions - www.lurpenaturalsolutions.com 🌱Substrate PRO-MIX HP BACILLUS + MYCORRHIZAE - www.pthorticulture.com/en/products/pro-mix-hp-biostimulant-plus-mycorrhizae

23.08 The Drainmaster moved into the tent to control the drain. Defoliated and lollipopped them. 25.08 First run with the drain system. Nutrient Solution (Tank): Volume: 8.5 L EC: 3.05 pH: 5.5 Nutrients: Advanced Nutrients Micro/Grow/Bloom + CalMag Irrigation Run: Pump time: 30 minutes Total Drain: 5.0 L (≈ 60%) Drain EC: 2.6 Drain pH: 6.0 🔎 Observations Drain volume was far too high (target is ~20%). Drain EC lower than input EC → medium was relatively “empty”, plants absorbed nutrients quickly. pH drift from 5.5 → 6.0 shows some buffering effect left in the reused substrate, but limited. Substrate behaves more like coco than soil now (low buffer, fast response). 💡 Insight / Lesson Learned 30 minutes pump time is way too long → resulted in 60% runoff instead of 20%. For 8 × 1 L pots, a single irrigation event should be ~1.0–1.2 L total, with ~200–250 ml runoff. Solution: shorten pump time to ~5 minutes and re-test runoff. Better approach: run shorter, more frequent irrigations (daily) with a lower EC (2.0–2.2), instead of heavy feedings (EC 3.0) only 3× per week. This will keep EC more stable in the root zone and prevent salt buildup in the tiny 1 L pots. 27.08 Adjusted the pump timer to 5 minutes, gave the first dose of PK13/14.

Week 13/5 - 19/5

minor bugs bites biting i have sticky traps i use Fox farm happy frog soil any advice for faster budding because i still don’t see any