c According to the Ramachandran plot. HMGâ 1 enhances HMGâ I/Y binding to an A/Tâ rich enhancer element from the pea plastocyanin gene Author: Webster, Carl I., Packman, Leonard C., Gray, John C. Source: European journal of biochemistry 2001 v.268 no.11 pp. Reviewed-Annotation score: -Experimental evidence at protein level i. View Answer. View Answer. The blue color of the oxidized protein is found to be due to the copper in a cupric combination with the protein moiety. bDegrees not included in total. Plastocyanin contains. Some cyanobacterial thylakoids also contain a caa3-type cytochrome c6 oxidase that requires three atoms of copper (1). 7A). The molar extinction coefficient (ε 597) of the copper chromophore was shown to be 4.5 x 10 3. The coordination sphere of the copper atom is comprised of two strongly bound histidine ligands and one cysteinate ligand. View Answer. In a situation of poor nutrition, organisms economize on the use of these elements by choosing alternate chemistries to achieve the same function. Pre-plastocyanin (Pre-PC), the precursor of plastocyanin, and Int-plastocyanin (Int-PC), the precursor of plastocyanin without its transit sequence, served as controls for import and localization. The spinach plastocyanin promoter contains most, if not all, cis elements crucial for its activity downstream of −259 by relative to the transcription start site. Copper 7. In addition to the beta-sheets, the structure contains an alpha-helix from Pro47 to Lys54 that follows beta-strand 4. 5). It is a "blue copper" protein. The following points highlight the top ten essential elements of Micronutrients. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.. Abundance. Iron: Iron is mainly absorbed by the plant in the ferrous form, but ferric ion may also be absorbed. Between 2 and 5 nmoles plastocyanin per mg chlorophyll are extracted (see also Ref. Reviewed-Annotation score: -Experimental evidence at protein level i. Cloning and characterization of the plastocyanin region. The Cu microRNAs, which are expressed during Cu deprivation, down-regulate several transcripts that encode for Cu proteins. It is estimated that approximately half of all proteins contain a metal. The plastocyanin contains some uncharacterized carbohydrate. View Answer. Plastocyanin is a key metalloprotein in the electron transfer processes from photosystem II to photosystem I. Plastocyanin consists of a polypeptide of approximate 100 amino acid residues and a type 1 copper atom (also called the “blue copper site”) coordinated by the side chains of four residues, two histidines, a cysteine, and a methionine. Manganese 3. the adaptive processes ( Cyc6 and Cpx1 transcription, plastocyanin degradation, copper transport) are targets of the same signal transduction pathway as is the case for Saccharomyces cerevisiae (see above). The endogenous plastocyanin (PC) concentrations of Dunaliella cultures were varied from 0.3 to 3.1 molecules per pigment 700 (P700) by decreasing the Cu+ supply of the nutrient. This plastocyanin is the smallest copper-protein yet reported; its molecular weight is 10,690. This model for the overall tumbling of plastocyanin provided a statistically significant improvement over the isotropic model, yielding an F statistic value of 4.7 for Cu(II) plastocyanin and of 5. Die back of shoots is due to . Many inorganic elements, because they are required for catalysis or as structural components in biomolecules, are essential nutrients for life. S/MARs contain sequences that strongly resemble the 21 bp DNA element found in S/MARs of the plastocyanin region. Plastocyanin was found in a head-on orientation, as determined using pseudocontact shifts, similar to that in the Phormidium complex, in which the hydrophobic patch represents the main site of interaction on plastocyanin. Based on the alignment of seven Arabidopsis S/MAR we propose Figure 1. plastocyanin from spinach chloroplasts by various methods. Treatment with Triton X-100 is most ef-fective. TATA and CCAAT boxes are located 34-bp and 68-bp, respectively, upstream of the transcription start de, the 5’-untranslated leader is 78 nucleotides long, and the intronless gene has at least two different polyadenylation sites. Zinc 6. In plants, the photosynthetic electron transport between the two photosystems has to cover distances of a few hundred nanometers. Immunoblots and mass spectrometric analysis of proteolytic peptides indicate that the two negative patches conserved in plant plastocyanins are cross-linked with lysine residues of a domain near the N-terminus of the PsaF subunit of photosystem I. View Answer. Biological energy conversion relies on a well-defined sequence of redox reactions within the membrane-embedded electron transport chains of chloroplasts and mitochondria. View Answer. Plastocyanin (Pc) is a copper-containing protein, which functions as an electron carrier between the cytochrome b(6)f and photosystem 1 (PS1) complexes in the photosynthetic electron transfer (ET) chain. Plastocyanin has 2 electron transfer paths. Reclamation and little leaf disease is caused by deficiency of. 1993 Dec; 4 (6):933–945. The amino acid composition of plastocyanin was determined. Gene. It is lacking cytochrome b-559, although three of the five polypeptides seem to carry heme groups. Plastocyanin, chloroplastic. Silicon. Our analysis of the 16 kb Arabidopsis plastocyanin region gives insight into the organisation of a region that contains a cluster of genes. The lateral distribution of plastocyanin in the thylakoid lumen of spinach and pea chloroplasts was studied by combining immunocytochemical localization and kinetic measurements of P700+ reduction at high time resolution. Photosystem I and plastocyanin can be cross-linked to an active electron transfer complex. The symerythrin and plastocyanin modules are largely associated with later Archean metabolisms, which include oxidation or aerobic pathways (Fig. In previous work, we showed that the Cyc6 gene contains at least two copper response elements (CuREs) (28). Boron 4. With these cultures the amount of PC which is sufficient for maximum photosynthesis in intact cells was determined to be about 1 to 1.5 PC/P700. Molybdenum 5. Cobalt 10. J. Biochem. Definition of plastocyanin An electron transferprotein, containing a type 1 copper site, involved in plant and cyanobacterial photosynthesis, which transfers electrons to … Copper is activator of enzyme. However, the interaction in the cross-complex is dependent on electrostatics, similar to that in the Nostoc complex. It does not contain plastocyanin and is almost completely devoid of chlorophyll and carotenoids, but lipid and detergent are present. PETE. Micronutrients Element # 1. The ET is mediated by His87 situated in the hydrophobic surface in the north region of Pc. The spinach plastocyanin promoter contains most, if not all, cis elements crucial for its activity downstream of -259 bp relative to the transcription start site. The elements arsenic, copper and mercury have which of the following effect? Plastocyanin, a photosynthetic electron transfer catalyst, is the most abundant copper protein in these organisms. The term microenvironment is used instead of fold or domain as these units often contain discontinuous elements of sequence and structure, ... use ferredoxin, cytochrome c, and plastocyanin modules. Background: Electron transfer between cytochrome f and photosystem I (PSI) can be accomplished by the heme-containing protein cytochrome c6 or by the copper-containing protein plastocyanin. Organism. An important question that can now be tackled is whether this organisation is related to the spatial and temporal expression pattern of the genes. The -259/-79 bp promoter fragment is capable of conferring glucuronidase (GUS) gene expression on the minimal -90/+3 bp 35S RNA promoter of CaMV and -51/+60 bp plastocyanin promoter, regardless of its orientation. Measurements were made by … Plastocyanin is imported into thylakoids as an unfolded protein (3), necessitating a separate copper supply to form the holoenzyme. 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