THYLAKOID ( PHOTOSYNTHESIS )
The word Thylakoid comes from the Greek word thylakos meaning "sac" or "pouch". Thus, thylakoid means "sac-like" or "pouch-like".
Structure
Thylakoids are membrane-bound structures embedded in the chloroplast stroma. A stack of thylakoids is called a granum and resembles a stack of coins.
Membrane
The thylakoid membrane is the site of the light-dependent reactions of photosynthesis with the photosynthetic pigments embedded directly in the membrane. It is an alternating pattern of dark and light bands measuring each 1 nanometre.
The thylakoid lipid bilayer shares characteristic features with prokaryotic membranes and the inner chloroplast membrane. For example, acidic lipids can be found in thylakoid membranes, cyanobacteria and other photosynthetic bacteria and are involved in the functional integrity of the photosystems.
The thylakoid membranes of higher plants are composed primarily of phospholipids and galactolipids that are asymmetrically arranged along and across the membranes. Thylakoid membranes are richer in galactolipids rather than phospholipids; also they predominantly consist of hexagonal phase II forming monogalacotosyl diglyceride lipid.
Despite this unique composition, plant thylakoid membranes have been shown to assume largely lipid-bilayer dynamic organization. Lipids forming the thylakoid membranes, richest in high-fluidity linolenic acid are synthesized in a complex pathway involving exchange of lipid precursors between the endoplasmic reticulum and inner membrane of the plastid envelope and transported from the inner membrane to the thylakoids via vesicles.
Lumen
The thylakoid lumen is a continuous aqueous phase enclosed by the thylakoid membrane. It plays an important role for photophosphorylation during photosynthesis. During the light-dependent reaction, protons are pumped across the thylakoid membrane into the lumen making it acidic down to pH 4.
Granum and stroma lamellae
In higher plants thylakoids are organized into a granum-stroma membrane assembly. A granum (plural grana) is a stack of thylakoid discs. Chloroplasts can have from 10 to 100 grana. Grana are connected by stroma thylakoids, also called intergranal thylakoids or lamellae. Grana thylakoids and stroma thylakoids can be distinguished by their different protein composition.
Grana contribute to chloroplasts' large surface area to volume ratio. Different interpretations of electron tomography imaging of thylakoid membranes has resulted in two models for grana structure. Both posit that lamellae intersect grana stacks in parallel sheets, though whether these sheets intersect in planes perpendicular to the grana stack axis, or are arranged in a right-handed helix is debated.
Formation
Chloroplasts develop from proplastids when seedlings emerge from the ground. Thylakoid formation requires light. In the plant embryo and in the absence of light, proplastids develop into etioplasts that contain semicrystalline membrane structures called prolamellar bodies. When exposed to light, these prolamellar bodies develop into thylakoids. This does not happen in seedlings grown in the dark, which undergo etiolation. An underexposure to light can cause the thylakoids to fail. This causes the chloroplasts to fail resulting in the death of the plant.
Thylakoid formation requires the action of vesicle-inducing protein in plastids 1 (VIPP1). Plants cannot survive without this protein, and reduced VIPP1 levels lead to slower growth and paler plants with reduced ability to photosynthesize. VIPP1 appears to be required for basic thylakoid membrane formation, but not for the assembly of protein complexes of the thylakoid membrane. It is conserved in all organisms containing thylakoids, including cyanobacteria, green algae, such as Chlamydomonas, and higher plants, such as Arabidopsis thaliana.
Isolation and fractionation
Thylakoids can be purified from plant cells using a combination of differential and gradient centrifugation.[14] Disruption of isolated thylakoids, for example by mechanical shearing, releases the lumenal fraction. Peripheral and integral membrane fractions can be extracted from the remaining membrane fraction. Treatment with sodium carbonate (Na2CO3) detaches peripheral membrane proteins, whereas treatment with detergents and organic solvents solubilizes integral membrane proteins.
Proteins
Thylakoid disc with embedded and associated proteins.
Thylakoids contain many integral and peripheral membrane proteins, as well as lumenal proteins. Recent proteomics studies of thylakoid fractions have provided further details on the protein composition of the thylakoids. These data have been summarized in several plastid protein databases that are available online.
According to these studies, the thylakoid proteome consists of at least 335 different proteins. Out of these, 89 are in the lumen, 116 are integral membrane proteins, 62 are peripheral proteins on the stroma side, and 68 peripheral proteins on the lumenal side.
Additional low-abundance lumenal proteins can be predicted through computational methods. Of the thylakoid proteins with known functions, 42% are involved in photosynthesis. The next largest functional groups include proteins involved in protein targeting, processing and folding with 11%, oxidative stress response (9%) and translation (8%).
Integral membrane proteins
Thylakoid membranes contain integral membrane proteins which play an important role in light harvesting and the light-dependent reactions of photosynthesis. There are four major protein complexes in the thylakoid membrane:
Photosystem II is located mostly in the grana thylakoids, whereas photosystem I and ATP synthase are mostly located in the stroma thylakoids and the outer layers of grana. The cytochrome b6f complex is distributed evenly throughout thylakoid membranes.
Due to the separate location of the two photosystems in the thylakoid membrane system, mobile electron carriers are required to shuttle electrons between them. These carriers are plastoquinone and plastocyanin. Plastoquinone shuttles electrons from photosystem II to the cytochrome b6f complex, whereas plastocyanin carries electrons from the cytochrome b6f complex to photosystem I.
Together, these proteins make use of light energy to drive electron transport chains that generate a chemiosmotic potential across the thylakoid membrane and NADPH, a product of the terminal redox reaction. The ATP synthase uses the chemiosmotic potential to make ATP during photophosphorylation.
These photosystems are light-driven redox centers, each consisting of an antenna complex that uses chlorophylls and accessory photosynthetic pigments such as carotenoids and phycobiliproteins to harvest light at a variety of wavelengths.
Each antenna complex has between 250 and 400 pigment molecules and the energy they absorb is shuttled by resonance energy transfer to a specialized chlorophyll a at the reaction center of each photosystem. When either of the two chlorophyll a molecules at the reaction center absorbs energy, an electron is excited and transferred to an electron-acceptor molecule.
Photosystem I contains a pair of chlorophyll a molecules, designated P700, at its reaction center that maximally absorbs 700 nm light. Photosystem II contains P680 chlorophyll that absorbs 680 nm light best (note that these wavelengths correspond to deep red – see the visible spectrum). The P is short for pigment and the number is the specific absorption peak in nanometers for the chlorophyll molecules in each reaction center.
The cytochrome b6f complex is part of the thylakoid electron transport chain and couples electron transfer to the pumping of protons into the thylakoid lumen. Energetically, it is situated between the two photosystems and transfers electrons from photosystem II-plastoquinone to plastocyanin-photosystem I.
The thylakoid ATP synthase is a CF1FO-ATP synthase similar to the mitochondrial ATPase. It is integrated into the thylakoid membrane with the CF1-part sticking into stroma. Thus, ATP synthesis occurs on the stromal side of the thylakoids where the ATP is needed for the light-independent reactions of photosynthesis.
Lumen proteins
The electron transport protein plastocyanin is present in the lumen and shuttles electrons from the cytochrome b6f protein complex to photosystem I. While plastoquinones are lipid-soluble and therefore move within the thylakoid membrane, plastocyanin moves through the thylakoid lumen.
The lumen of the thylakoids is also the site of water oxidation by the oxygen evolving complex associated with the lumenal side of photosystem II.
Lumenal proteins can be predicted computationally based on their targeting signals. In Arabidopsis, out of the predicted lumenal proteins possessing the Tat signal, the largest groups with known functions are 19% involved in protein processing (proteolysis and folding), 18% in photosynthesis, 11% in metabolism, and 7% redox carriers and defense.
Protein expression
Chloroplasts have their own genome, which encodes a number of thylakoid proteins. However, during the course of plastid evolution from their cyanobacterial endosymbiotic ancestors, extensive gene transfer from the chloroplast genome to the cell nucleus took place. This results in the four major thylakoid protein complexes being encoded in part by the chloroplast genome and in part by the nuclear genome.
Plants have developed several mechanisms to co-regulate the expression of the different subunits encoded in the two different organelles to assure the proper stoichiometry and assembly of these protein complexes.
For example, transcription of nuclear genes encoding parts of the photosynthetic apparatus is regulated by light. Biogenesis, stability and turnover of thylakoid protein complexes are regulated by phosphorylation via redox-sensitive kinases in the thylakoid membranes.
The translation rate of chloroplast-encoded proteins is controlled by the presence or absence of assembly partners (control by epistasy of synthesis). This mechanism involves negative feedback through binding of excess protein to the 5' untranslated region of the chloroplast mRNA.
Chloroplasts also need to balance the ratios of photosystem I and II for the electron transfer chain. The redox state of the electron carrier plastoquinone in the thylakoid membrane directly affects the transcription of chloroplast genes encoding proteins of the reaction centers of the photosystems, thus counteracting imbalances in the electron transfer chain.
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