En 2 Semanas un crecimiento Notable. Las plantas llevan 17 Días. Una de las tres en la que más representa al banco BSF. La más BIgger Stronger y Faster.

Back Again , well the FBT09/Sour Diesel plants are looking fine . The normal plant is looking really good and has very distinct spiked leaves . It also has a slightly tighter internodal spacing than the its sisters all except for Tester 2 which is the bushiest. The other plant (polyploid) is also bushy but in a mutant abstract type growth pattern , It has two heads even tho I never topped it . 👽 This is a Freaky plant hope it produces some freaky Buds 😝 I gave the girls a feed of Mr B's Green Trees Bloom Mix (third of a cup per pot) and a qtr tspoon of Great White. Thats it for this weeks update Be Back Next Year.👍

Still giving me a little stretch this week which is fine because there’s still some room. I initially thought they were going to get a bit taller or I might have waited another few days. Either way there’s a TON of cola sites and I’ve selectively removed a few fan leaves blocking them. I turned up the HLG 550v2 to about 90% power and switched the nutes to a higher phosphorus and less nitrogen base. All In all everything is on track.

Plants were a little neglected this week due to health issues. Temps are cooler also which is not helping with growth, but they are still doing well

She is in full flower now, I change the nutriënts to flower and removed all the lower grow.

Wow my first grow

Procede tutto egregiamente. Son riuscito a coprire la rete quasi per intero. La punta di alcune foglie si stanno ingiallendo, ma non è importante visto che siamo quasi vicino al raccolto. Inizio della seconda settimana senza nutriente per pulire le piante. Spera che la prossima settimana sia di raccolto. Saluti (A)narchici 🖤❤️ Doctor Cannas

Aug 24: starting the sixth week of flowering and she’s looking pretty good. Trichomes are developing and the buds are thickening. So far so good. Aug 27: looking close to ready but I’m not in a hurry. Will see in a week or two how it’s progressing.

All the Pheno’s are green and healthy, Indoors was overwatered or the substrate got too cold. I started seeing what looked like Iron lock out(pale yellow/whitish color on the new growth’s basal leaflet). I reduced the frequency of the added Coconut water powder and Aloe Vera powder and allowed the substrate to heat up to above 72 degrees Fahrenheit(was 68F) and now the new growth is turning a vibrant green again. #1 and #4 are my favorite out of the outdoor and indoor sisters. The indoor plants started showing sex on April 18th 2022, still waiting on outdoors to show sex.

Heya👍🤙👍🌱 Flower away!!! Check out my Facebook profile: https://www.facebook.com/share/v/H6PnoahTHrEzm63U/?mibextid=oFDknk Big BIG BIG thank you to Sebastien, Heather from Fastbuds420. You guys are the best. Can't wait for the next live. Even Bigger shout out to Hydroponic.co.za. My local Hydro Shop and Sponsor. Thank you Sir. 👍🤙👍🌱

This will be a bit of a challenge, one of the LCC is 45cm while the others are 25cm. I gave them little ramps to keep canopy even and all 3 are still looking healthy.

One Bud was moldy where the other plants had no issues. This strain might me a little susceptible to mold. The Terps on this are very nice. Dark Grape with hints of lemon. Very Sticky and not very hard Trichome shells. maybe good for flower rosin or under cold contidions even for Hash Rosin.

Uz uz to bude

On day 6 week 4 She is putting out alot of pistills and budlets no smell yet.flowering is deff underway now. This is looking like a 10 week strain as she took almost 4 weeks to start budlets which I usually see around week 2-3.

Trichomes trichomes !! What a beautiful plant 🌱 to grow , not big bud producers but absolutely coated.u can definitely tell it’s got the GCS in her , Terps are getting stronger now that really forum cut Girl Scout cookies terps with some creamy peanut tons . The stretch is about over now

12.03.2024 – Ein Desaster mit Hoffnung Wo fange ich an, wo höre ich auf…? In diesem Zeitraum bin ich umgezogen und musste mir überlegen, wie ich das Ganze manage, damit die Ernte am Ende optimal wird – was sie leider nicht wurde.😅 Die Pflanze war genau in der Zeit fertig, als ich mit meinem Umzug beschäftigt war und in den Urlaub geflogen bin. Also entschied ich mich dazu, sie vor meiner Abreise zu köpfen und aufzuhängen. Eigentlich wollte ich die gesamte Ernte wieder in DryFerms trocknen lassen, doch da ich mein Zeitmanagement dieses Mal überhaupt nicht im Griff hatte, wurde alles ziemlich kurzfristig. Die Buds mussten ja auch vorher noch getrimmt werden. Also ließ ich das bleiben und hängte sie einfach auf. In meiner neuen Wohnung stellte ich schon mal ein Hygrometer auf, um die relative Luftfeuchtigkeit zu checken – 42 %. Schon ziemlich trocken, aber ich dachte mir nichts weiter dabei. Wird schon irgendwie klappen... Dann flog ich in den Urlaub. Fünf Tage später war ich zurück. Die Ernte hing bereits einen Tag vor meiner Abreise. Als ich mein Zelt öffnete, sah ich das Desaster kommen: Das Hygrometer zeigte eine RLF von nur 32 % an. Die Buds waren staubtrocken. Die ganze Arbeit – für nichts. Besonders ärgerlich, denn von allen drei Pflanzen war diese die vielversprechendste, sowohl was die Terpene als auch den Ertrag betrifft. Ich war kurz davor, alles wegzuschmeißen, weil ich mir das Elend nicht mehr anschauen konnte. Schlussendlich entschied ich mich aber doch dazu, die Ernte so gut es ging zu trimmen. Ein Desaster, das kann ich euch sagen! Die Hälfte aller Buds löste sich in Staub auf – kaum setzte ich die Schere an, zerfielen sie. Am Ende blieben mir doch noch 32 g, allerdings extrem empfindlich. Curing? Keine Chance. Trotzdem wollte ich das Beste herausholen. Also packte ich die Ernte mit zwei Bovedas für sechs Tage in ein Glas – und siehe da: Die Buds nahmen die Feuchtigkeit auf, die sie brauchten! Am Ende hatte ich zumindest halbwegs vernünftiges Material. Jetzt lagert alles in Grove Bags mit einem Boveda und wird genau beobachtet. Ich hoffe, dass daraus noch gutes, rauchbares Material wird! Eins ist sicher: Die Dosidos Auto wird auf jeden Fall noch mal gegrowt – und dann richtig ✊!

just about finished up this week. Choc mint 1 is about ready for chop. Chopped couple of main colas as i seen couple of signs of budrot. Dropped lights down to 400w each as temps are starting to rise above 30c. Choc mint 2 is looking unreal. Heaps of huge colas,think i will pull the most of this one. Will probably give till day 65.

First Week of flowering Week without too much hassle. A small excess of fertilizer but nothing serious. Uniform color. High water consumption (10L every 2 days), you can feel that they are in good shape. Semaine sans trop d'encombre. Un petit excès de fertilisant mais rien de grave. Couleur uniforme. Grosse consommation en eau (10L tous les 2 jours), on sent qu'elles sont en forme. Una semana sin demasiados problemas. Un poco de exceso de fertilizante pero nada serio. Color uniforme. El alto consumo de agua (10L cada 2 días), se puede sentir que están en buena forma.

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.