Journal articles: 'Chlorophyll a/b binding proteins'

1

Paulsen, Harald. "CHLOROPHYLL a/b-BINDING PROTEINS." Photochemistry and Photobiology 62, no. 3 (September 1995): 367–82. http://dx.doi.org/10.1111/j.1751-1097.1995.tb02357.x.

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Bassi, Roberto, Dorianna Sandona, and Roberta Croce. "Novel aspects of chlorophyll a/b-binding proteins." Physiologia Plantarum 100, no. 4 (August 1997): 769–79. http://dx.doi.org/10.1034/j.1399-3054.1997.1000404.x.

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Bassi, Roberto, Dorianna Sandona, and Roberta Croce. "Novel aspects of chlorophyll a/b-binding proteins." Physiologia Plantarum 100, no. 4 (August 1997): 769–79. http://dx.doi.org/10.1111/j.1399-3054.1997.tb00004.x.

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4

Green, Beverly R., Eran Pichersky, and Klaus Kloppstech. "Chlorophyll a/b-binding proteins: an extended family." Trends in Biochemical Sciences 16 (January 1991): 181–86. http://dx.doi.org/10.1016/0968-0004(91)90072-4.

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Krol, M., M. D. Spangfort, NPA Huner, G. Oquist, P. Gustafsson, and S. Jansson. "Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant." Plant Physiology 107, no. 3 (March 1, 1995): 873–83. http://dx.doi.org/10.1104/pp.107.3.873.

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Van Buren, Jerome P. "Extraction of chlorophylls a and b from different binding sites on thylakoid chlorophyll-proteins." Journal of Agricultural and Food Chemistry 33, no. 2 (March 1985): 204–8. http://dx.doi.org/10.1021/jf00062a011.

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7

Babiychuk, Elena, Rodolphe Schantz, Nicolai Cherep, Jacques-Henry Weil, Yuri Gleba, and Sergei Kushnir. "Alterations in chlorophyll a/b binding proteins in Solanaceae cybrids." Molecular and General Genetics MGG 249, no. 6 (November 1995): 648–54. http://dx.doi.org/10.1007/bf00418034.

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8

H�yer-Hansen, G., R. Bassi, L. S. H�nberg, and D. J. Simpson. "Immunological characterization of chlorophyll a/b-binding proteins of barley thylakoids." Planta 173, no. 1 (January 1988): 12–21. http://dx.doi.org/10.1007/bf00394481.

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9

Darr, S. C., S. C. Somerville, and C. J. Arntzen. "Monoclonal antibodies to the light-harvesting chlorophyll a/b protein complex of photosystem II." Journal of Cell Biology 103, no. 3 (September 1, 1986): 733–40. http://dx.doi.org/10.1083/jcb.103.3.733.

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A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity. Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor. Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that there are structural similarities among the polypeptides of LHC-II and LHC-I. The evidence for protein processing by which the 26-, 25.5-, and 24.5-kD polypeptides are derived from a common precursor polypeptide is discussed. Binding studies using antibodies specific for individual LHC-II polypeptides were used to quantify the number of antigenic polypeptides in the thylakoid membrane. 27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls. In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected. We propose that stable insertion and assembly of the 28-kD polypeptide, unlike the 26-kD polypeptide, is not regulated by the presence of chlorophyll b.

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Allen, K. D., M. E. Duysen, and L. A. Staehelin. "Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat." Journal of Cell Biology 107, no. 3 (September 1, 1988): 907–19. http://dx.doi.org/10.1083/jcb.107.3.907.

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Biogenesis of thylakoid membranes in the conditional chlorophyll b-deficient CD3 mutant of wheat is dramatically altered by relatively small differences in the light intensity under which seedlings are grown. When the CD3 mutant is grown at 400 microE/m2 S (high light, about one-fifth full sunlight) plants are deficient in chlorophyll b (chlorophyll a/b ratio greater than 6.0) and lack or contain greatly reduced amounts of the chlorophyll a/b-binding complexes CPII/CPII (mobile or peripheral LHCII), CP29, CP24 and LHCI, as shown by mildly denaturing 'green gel' electrophoresis, by fully denaturing SDS-PAGE, and by Western blot analysis. High light CD3 chloroplasts display an unusual morphology characterized by large, sheet-like stromal thylakoids formed into parallel unstacked arrays and a limited number of small grana stacks displaced toward the edges of the arrays. Changes in the supramolecular organization of CD3 thylakoids, seen with freeze-fracture electron microscopy, include a reduction in the size of EFs particles, which correspond to photosystem II centers with variable amounts of attached LHCII, and a redistribution of EF particles from the stacked to the unstacked regions. When CD3 seedlings are grown at 150 microE/m2 S (low light) there is a substantial reversal of all of these effects. Thus, chlorophyll b and the chlorophyll a/b-binding proteins accumulate to near wild-type levels (chlorophyll a/b ratio = 3.5-4.5) and thylakoid morphology is more nearly wild type in appearance. Growth of the CD3 mutant in the presence of chloramphenicol stimulates the accumulation of chlorophyll b and its binding proteins (Duysen, M. E., T. P. Freeman, N. D. Williams, and L. L. Huckle. 1985. Plant Physiol. 78:531-536). We show that this partial rescue of the CD3 high light phenotype is accompanied by large changes in thylakoid structure. The CD3 mutant, which defines a new class of chlorophyll b-deficient phenotype, is discussed in the more general context of chlorophyll b deficiency.

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El Rabey, Haddad A., Abdulrahman L. Al-Malki, Khalid O. Abulnaja, and Wolfgang Rohde. "Proteome Analysis for Understanding Abiotic Stress (Salinity and Drought) Tolerance in Date Palm (Phoenix dactyliferaL.)." International Journal of Genomics 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/407165.

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This study was carried out to study the proteome of date palm under salinity and drought stress conditions to possibly identify proteins involved in stress tolerance. For this purpose, three-month-old seedlings of date palm cultivar “Sagie” were subjected to drought (27.5 g/L polyethylene glycol 6000) and salinity stress conditions (16 g/L NaCl) for one month. DIGE analysis of protein extracts identified 47 differentially expressed proteins in leaves of salt- and drought-treated palm seedlings. Mass spectrometric analysis identified 12 proteins; three out of them were significantly changed under both salt and drought stress, while the other nine were significantly changed only in salt-stressed plants. The levels of ATP synthase alpha and beta subunits, an unknown protein and some of RubisCO fragments were significantly changed under both salt and drought stress conditions. Changes in abundance of superoxide dismutase, chlorophyll A-B binding protein, light-harvesting complex1 protein Lhca1, RubisCO activase, phosphoglycerate kinase, chloroplast light-harvesting chlorophyll a/b-binding protein, phosphoribulokinase, transketolase, RubisCO, and some of RubisCO fragments were significant only for salt stress.

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Shinohara, Kenji, Naoki Yamamoto, Yuzuru Mukai, and Keiji Odani. "Biogenesis pathway of pine chloroplast proteins encoded in the nucleus: import of pine proteins into spinach chloroplasts." Canadian Journal of Forest Research 24, no. 2 (February 1, 1994): 419–23. http://dx.doi.org/10.1139/x94-056.

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Precursors to small subunits (SSU) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) and apoproteins of light-harvesting chlorophyll a/b binding protein (LHCPII) in photosystem II were synthesized in vitro by expressing pine (Pinus thunbergii Parl.) cDNA clones encoding these proteins. The precursors to pine SSU and LHCPII were post-translationally transported into spinach chloroplasts, processed into mature size, and localized in only stroma and thylakoid membranes, respectively. The pine SSU was tightly integrated into spinach Rubisco; however, the pine LHCPII was not found in the light-harvesting chlorophyll–protein complex. These results suggest that a common biogenesis pathway of nuclear-encoded chloroplast proteins is present both in gymnosperms and in angiosperms.

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13

Evans, JR. "Acclimation by the Thylakoid Membranes to Growth Irradiance and the Partitioning of Nitrogen Between Soluble and Thylakoid Proteins." Functional Plant Biology 15, no. 2 (1988): 93. http://dx.doi.org/10.1071/pp9880093.

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Three characteristics of shade plants are reviewed. Firstly, they have relatively more chlorophyll b and the associated light-harvesting chlorophyll a/b-protein complex (LHC). Two currently accepted reasons for this are not supported by quantitative analysis. Instead, the reduced protein cost of complexing chlorophyll in LHC and the turnover of the 32 kDa herbicide binding protein are considered. Secondly, shade plants have low electron transport capacities per unit of chlorophyll. This is primarily related to a reduction in the amount of electron transport components such as the cytochrome f complex and the ATPase. The nitrogen cost of the thylakoid membranes per unit of light absorbed is thereby reduced, but the irradiance range over which light is used with high efficiency is also reduced. Thirdly, shade plants have less RuP2 carboxylase and other soluble proteins for a given amount of chlorophyll. However, while the ratio of RuP2 carboxylase protein to thylakoid protein declined, the ratio of the RuP2 carboxylase activity to electron transport activity increased. For several species, the relationship between the rate of CO2 assimilation and leaf nitrogen content depends on the irradiance during growth.

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14

Lamppa, G. K., G. Morelli, and N. H. Chua. "Structure and developmental regulation of a wheat gene encoding the major chlorophyll a/b-binding polypeptide." Molecular and Cellular Biology 5, no. 6 (June 1985): 1370–78. http://dx.doi.org/10.1128/mcb.5.6.1370.

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A genomic clone for a major chlorophyll a/b-binding polypeptide of the light-harvesting complex has been sequenced from wheat. This gene, whAB1.6, encodes a 70-nucleotide 5'-nontranslated spacer, a 34-amino-acid NH2-terminal extension, i.e., the transit peptide, and a mature coding protein of 232 amino acid residues. The exact molecular weight of the precursor polypeptide is 28,560. The transit peptide is basic and is rich in serines. No intervening sequences are found in this gene. The transcription start site of the whAB1.6 gene occurs at AAAC as determined by S1 nuclease analysis. Putative regulatory sequences occur upstream of the gene at -25 (TTTAAATA) and at -72 (CCAACCA). Northern blots show a single RNA species estimated to be 1,100 nucleotides. Heterogeneity of the RNA population is demonstrated in S1 nuclease analyses with a 5'-end-labeled fragment that extends 191 nucleotides into the mature protein coding sequence. At least seven different transcripts can be recognized. The highest levels of RNA transcribed from the whAB1.6 gene are found in the basal segments of the wheat leaf, whereas other chlorophyll a/b-binding transcripts in the cell show a different pattern of abundance. As a control, we show that roots do not contain chlorophyll a/b-binding RNA. The most abundant RNA species shows an interrupted homology with the whAB1.6 gene at the start of the mature protein coding sequence; another species shows homology beginning at the start of the transit peptide and does not include the nontranslated region. Chlorophyll a/b-binding polypeptides accumulate toward the tip of the leaf as shown by Western blot analysis of total thylakoid proteins.

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Lamppa, G. K., G. Morelli, and N. H. Chua. "Structure and developmental regulation of a wheat gene encoding the major chlorophyll a/b-binding polypeptide." Molecular and Cellular Biology 5, no. 6 (June 1985): 1370–78. http://dx.doi.org/10.1128/mcb.5.6.1370-1378.1985.

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A genomic clone for a major chlorophyll a/b-binding polypeptide of the light-harvesting complex has been sequenced from wheat. This gene, whAB1.6, encodes a 70-nucleotide 5'-nontranslated spacer, a 34-amino-acid NH2-terminal extension, i.e., the transit peptide, and a mature coding protein of 232 amino acid residues. The exact molecular weight of the precursor polypeptide is 28,560. The transit peptide is basic and is rich in serines. No intervening sequences are found in this gene. The transcription start site of the whAB1.6 gene occurs at AAAC as determined by S1 nuclease analysis. Putative regulatory sequences occur upstream of the gene at -25 (TTTAAATA) and at -72 (CCAACCA). Northern blots show a single RNA species estimated to be 1,100 nucleotides. Heterogeneity of the RNA population is demonstrated in S1 nuclease analyses with a 5'-end-labeled fragment that extends 191 nucleotides into the mature protein coding sequence. At least seven different transcripts can be recognized. The highest levels of RNA transcribed from the whAB1.6 gene are found in the basal segments of the wheat leaf, whereas other chlorophyll a/b-binding transcripts in the cell show a different pattern of abundance. As a control, we show that roots do not contain chlorophyll a/b-binding RNA. The most abundant RNA species shows an interrupted homology with the whAB1.6 gene at the start of the mature protein coding sequence; another species shows homology beginning at the start of the transit peptide and does not include the nontranslated region. Chlorophyll a/b-binding polypeptides accumulate toward the tip of the leaf as shown by Western blot analysis of total thylakoid proteins.

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Boivin, Rodolphe, Diane Beauseigle, Chris L. Baszczynski, and Guy Bellemare. "Isolation of Lhcb3 sequences from Brassica napus: evidence for conserved genes encoding LHCII type III chlorophyll a/b binding proteins." Genome 36, no. 1 (February 1, 1993): 139–46. http://dx.doi.org/10.1139/g93-017.

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Three closely related sequences were isolated from Brassica napus genomic DNA and were identified as Lhcb3 (genes encoding type III chlorophyll a/b binding proteins of LHCII, the major light-harvesting complex of photosystem II). These genes, as was observed for a tomato Lhcb3, contain two introns and yield both divergent and conserved predicted amino acid segments as compared with type I and type II polypeptides. One of the B. napus genes, designated Lhcb3*1, is transcribed in vivo, since it is identical to corresponding sequences in a cDNA clone. The protein deduced from another sequence, Lhcb3*2, appears as the most divergent type III so far characterized. The partial sequence of a third gene, Lhcb3*3, was also recovered. The 5′ noncoding sequences of Lhcb3*1 and Lhcb3*2, in the far upstream region, are characterized by an extremely high AT content and extensive direct repeats. In the near upstream region, two long Lhcb3*2 segments are very similar to a segment proposed as containing regulatory signals in Lhcb3*1. Specific binding of nuclear proteins to Lhcb3*1 promoter fragments was detected by electrophoretic mobility-shift assays. The evolutionary relationship between genes for type III polypeptides and the other types present in LHCII is discussed.Key words: Brassica napus, chlorophyll a/b binding proteins, LHCII type III, promoter region, lhcb genes evolution.

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17

Kilian, Roswitha, Roberto Bassi, and Christian Schäfer. "Identification and characterization of photosystem II chlorophyll a / b binding proteins in Marchantia polymorpha L." Planta 204, no. 2 (January 22, 1998): 260–67. http://dx.doi.org/10.1007/s004250050255.

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Hasegawa, Keiko, Yasushi Yukawa, Mamoru Sugita, and Masahiro Sugiura. "Organization and transcription of the gene family encoding chlorophyll a/b -binding proteins in Nicotiana sylvestris." Gene 289, no. 1-2 (May 2002): 161–68. http://dx.doi.org/10.1016/s0378-1119(02)00539-5.

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19

Boichenko, Vladimir A., Alexander V. Pinevich, and Igor N. Stadnichuk. "Association of chlorophyll a/b-binding Pcb proteins with photosystems I and II in Prochlorothrix hollandica." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1767, no. 6 (June 2007): 801–6. http://dx.doi.org/10.1016/j.bbabio.2006.11.001.

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20

Oba, Toru, and Hitoshi Tamiaki. "Asymmetry of chlorophylls in photosynthetic proteins: from the viewpoint of coordination chemistry." Journal of Porphyrins and Phthalocyanines 18, no. 10n11 (October 2014): 919–32. http://dx.doi.org/10.1142/s1088424614500710.

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We conducted a meta-analysis of (bacterio)chlorophyll [(B)Chl] molecules in photosynthetic pigment-protein complexes from the viewpoint of coordination chemistry. We surveyed the ligand species and site in the axial coordination of 146 Chl and 21 BChl molecules in 42 reported crystal structures of 12-type proteins. The imidazolyl moiety of histidine (His) is the most abundant ligand, and the second is water, a much weaker ligand. We focused on the positions, the circumstances, and the macrocycle sides for the coordination of the 31 hydrated (B)Chl molecules found in these proteins. A ligand water molecule of a hydrated (B)Chl is not necessarily hydrogen-bonded to the surrounding protein residues. A hydrated (B)Chl seems to occupy the redundant space where more strongly coupled His-Chl complexes cannot be formed. It is noted that 28 of 31 hydrated (B)Chl molecules (90) were coordinated from the α-side of the (bacterio)chlorin macrocycle, the opposite side from which the C 17-propionic ester protrudes. Among them, all five hydrated Chl molecules at the edges of the proteins were coordinated from the α-side, suggesting that (B)Chl molecules prefer this side for the coordination bondings to the β-side. The analysis also revealed that each (B)Chl binding site was composed of both the protein residues and the neighboring pigment molecules contributing roughly equally. It can be safely said that the cofactor pigments aggregated even in the proteins. Penta-coordination is advantageous to flexible adjustment of intermolecular orientations of (B)Chl molecules in the aggregates.

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JAHNS, Peter, and Wolfgang JUNGE. "Dicyclohexylcarbodiimide-binding proteins related to the short circuit of the proton-pumping activity of photosystem II. Identified as light-harvesting chlorophyll-a/b-binding proteins." European Journal of Biochemistry 193, no. 3 (November 1990): 731–36. http://dx.doi.org/10.1111/j.1432-1033.1990.tb19393.x.

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22

Sigrist, Markus, and L. Andrew Staehelin. "Identification of type 1 and type 2 light-harvesting chlorophyll a/b-binding proteins using monospecific antibodies." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1098, no. 2 (January 1992): 191–200. http://dx.doi.org/10.1016/s0005-2728(05)80336-6.

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23

Jahns, P. "The Xanthophyll Cycle in Intermittent Light-Grown Pea Plants (Possible Functions of Chlorophyll a/b-Binding Proteins)." Plant Physiology 108, no. 1 (May 1, 1995): 149–56. http://dx.doi.org/10.1104/pp.108.1.149.

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Dolganov, N. A., D. Bhaya, and A. R. Grossman. "Cyanobacterial protein with similarity to the chlorophyll a/b binding proteins of higher plants: evolution and regulation." Proceedings of the National Academy of Sciences 92, no. 2 (January 17, 1995): 636–40. http://dx.doi.org/10.1073/pnas.92.2.636.

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25

Xu, Yan-Hong, Rui Liu, Lu Yan, Zhi-Qiang Liu, Shang-Chuan Jiang, Yuan-Yue Shen, Xiao-Fang Wang, and Da-Peng Zhang. "Light-harvesting chlorophyll a/b-binding proteins are required for stomatal response to abscisic acid in Arabidopsis." Journal of Experimental Botany 63, no. 3 (December 5, 2011): 1095–106. http://dx.doi.org/10.1093/jxb/err315.

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26

Giardi, M. T., J. Barber, M. C. Giardina, and R. Bassi. "Studies on the Herbicide Binding Site in Isolated Photosystem II Core Complexes from a Flat-Bed Isoelectrofocusing Method." Zeitschrift für Naturforschung C 45, no. 5 (May 1, 1990): 366–72. http://dx.doi.org/10.1515/znc-1990-0510.

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Abstract Isoelectrofocusing has been used to separate various chlorophyll-protein complexes of photosystem two (PS II). Light-harvesting complexes containing chlorophyll a and chlorophyll b (LHC II) were located in bands having p/s in the region of 4.5. At slightly higher pH other light-harvesting complexes containing little or no chlorophyll b were found. In the most basic region of the isoelectrofocusing gel, were located PS II core complexes characterized by containing the proteins of CP47, CP43, D 1, D 2 and α-subunit of cytochrome b559. The number of PS II core bands depended on the particular conditions employed for the separation procedure and in some cases were contaminated by CP 29. It is suggested that this heterogeneity resulting from different protonation states of the PS II. The least-acidic PS II core complex (pI 5.5) was found to bind the herbicides atrazine, diuron and dinoseb. In contrast, a PS II core complex with a p / of 4.9 bound only diuron. Its inability to bind atrazine was shown to be due to the low pH but no such explanation could be found for dinoseb. When atrazine-resistant mutant Senecio vulgaris was used, no binding of radioactive atra zine was observed with the PS II cores having a p i of 5.5. It is therefore suggested that the normal atrazine binding observed with PS II cores involves the high affinity site detected with intact membranes. With the PS II cores, however, this site has a reduced affinity probably due to structural modification in the D 1-polypeptide resulting from the isolation procedures.

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Song, Guo-qing, Hideo Honda, and Ken-ichi Yamaguchi. "Expression of a Rice Chlorophyll a/b Binding Protein Promoter in Sweetpotato." Journal of the American Society for Horticultural Science 132, no. 4 (July 2007): 551–56. http://dx.doi.org/10.21273/jashs.132.4.551.

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Leaves are usually the target tissue for expressing transgenes conferring resistances to herbicides, pests, and diseases. To achieve leaf-specific expression, a light-harvest chlorophyll a/b binding protein (CAB) of photosystem-II (CAB2) promoter (CAB2-p) from rice (Oryza sativa L.) and the cauliflower mosaic virus 35S promoter were fused to the β-glucuronidase (GUS) reporter and subsequently evaluated in transgenic sweetpotato [Ipomoea batatas L. (Lam.)]. The 35S promoter-directed GUS activities varied from 46.0 to 61.2 nmol 4-methyl-umbelliferyl-β-D-glucuronide (4-MU) per minute per milligram of protein in leaf, stem, primary, and storage roots. In contrast, the CAB2-p directed an uneven distribution of GUS activities (4-MU at 1.1 to 12.6 nmol·min−1·mg−1 protein); GUS activity in mature leaves was ≈12-fold as high as that in storage roots. In addition, GUS assay in leaf tissues revealed that CAB2-p enabled a developmentally controlled and light-regulated GUS expression. These results indicate that the rice CAB2-p could be used to drive leaf-specific expression of linked genes in sweetpotato.

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Kume, Atsushi, Tomoko Akitsu, and Kenlo Nishida Nasahara. "Why is chlorophyll b only used in light-harvesting systems?" Journal of Plant Research 131, no. 6 (July 10, 2018): 961–72. http://dx.doi.org/10.1007/s10265-018-1052-7.

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Abstract Chlorophylls (Chl) are important pigments in plants that are used to absorb photons and release electrons. There are several types of Chls but terrestrial plants only possess two of these: Chls a and b. The two pigments form light-harvesting Chl a/b-binding protein complexes (LHC), which absorb most of the light. The peak wavelengths of the absorption spectra of Chls a and b differ by c. 20 nm, and the ratio between them (the a/b ratio) is an important determinant of the light absorption efficiency of photosynthesis (i.e., the antenna size). Here, we investigated why Chl b is used in LHCs rather than other light-absorbing pigments that can be used for photosynthesis by considering the solar radiation spectrum under field conditions. We found that direct and diffuse solar radiation (PARdir and PARdiff, respectively) have different spectral distributions, showing maximum spectral photon flux densities (SPFD) at c. 680 and 460 nm, respectively, during the daytime. The spectral absorbance spectra of Chls a and b functioned complementary to each other, and the absorbance peaks of Chl b were nested within those of Chl a. The absorption peak in the short wavelength region of Chl b in the proteinaceous environment occurred at c. 460 nm, making it suitable for absorbing the PARdiff, but not suitable for avoiding the high spectral irradiance (SIR) waveband of PARdir. In contrast, Chl a effectively avoided the high SPFD and/or high SIR waveband. The absorption spectra of photosynthetic complexes were negatively correlated with SPFD spectra, but LHCs with low a/b ratios were more positively correlated with SIR spectra. These findings indicate that the spectra of the photosynthetic pigments and constructed photosystems and antenna proteins significantly align with the terrestrial solar spectra to allow the safe and efficient use of solar radiation.

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Kwon, Soon-Wook, Mijeong Kim, Hijin Kim, and Joohyun Lee. "Shotgun Quantitative Proteomic Analysis of Proteins Responding to Drought Stress inBrassica rapaL. (Inbred Line “Chiifu”)." International Journal of Genomics 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/4235808.

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Through a comparative shotgun quantitative proteomics analysis inBrassica rapa(inbred line Chiifu), total of 3,009 nonredundant proteins were identified with a false discovery rate of 0.01 in 3-week-old plants subjected to dehydration treatment for 0, 24, and 48 h, plants subjected to drought stress. Ribulose-bisphosphate carboxylases, chlorophyll a/b-binding protein, and light harvesting complex in photosystem II were highly abundant proteins in the leaves and accounted for 9%, 2%, and 4%, respectively, of the total identified proteins. Comparative analysis of the treatments enabled detection of 440 differentially expressed proteins during dehydration. The results of clustering analysis, gene ontology (GO) enrichment analysis, and analysis of composite expression profiles of functional categories for the differentially expressed proteins indicated that drought stress reduced the levels of proteins associated with photosynthesis and increased the levels of proteins involved in catabolic processes and stress responses. We observed enhanced expression of many proteins involved in osmotic stress responses and proteins with antioxidant activities. Based on previously reported molecular functions, we propose that the following five differentially expressed proteins could provide target genes for engineering drought resistance in plants: annexin, phospholipase D delta, sDNA-binding transcriptional regulator, auxin-responsive GH3 family protein, and TRAF-like family protein.

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Liang, Fu-Cheng, Gerard Kroon, Camille Z. McAvoy, Chris Chi, Peter E. Wright, and Shu-ou Shan. "Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release." Proceedings of the National Academy of Sciences 113, no. 12 (March 7, 2016): E1615—E1624. http://dx.doi.org/10.1073/pnas.1524777113.

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Membrane protein biogenesis poses enormous challenges to cellular protein homeostasis and requires effective molecular chaperones. Compared with chaperones that promote soluble protein folding, membrane protein chaperones require tight spatiotemporal coordination of their substrate binding and release cycles. Here we define the chaperone cycle for cpSRP43, which protects the largest family of membrane proteins, the light harvesting chlorophyll a/b-binding proteins (LHCPs), during their delivery. Biochemical and NMR analyses demonstrate that cpSRP43 samples three distinct conformations. The stromal factor cpSRP54 drives cpSRP43 to the active state, allowing it to tightly bind substrate in the aqueous compartment. Bidentate interactions with the Alb3 translocase drive cpSRP43 to a partially inactive state, triggering selective release of LHCP’s transmembrane domains in a productive unloading complex at the membrane. Our work demonstrates how the intrinsic conformational dynamics of a chaperone enables spatially coordinated substrate capture and release, which may be general to other ATP-independent chaperone systems.

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Umate, Pavan. "Genome-wide analysis of the family of light-harvesting chlorophyll a/b-binding proteins in Arabidopsis and rice." Plant Signaling & Behavior 5, no. 12 (December 2010): 1537–42. http://dx.doi.org/10.4161/psb.5.12.13410.

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32

Wolf, Andreas H., Annette Br�dern, Martin Giersberg, and Wolfgang Wiessner. "Influence of photoheterotrophy on the expression of chlorophyll a/b-binding proteins in the green alga Pyrobotrys stellata." Photosynthesis Research 49, no. 1 (July 1996): 49–56. http://dx.doi.org/10.1007/bf00029427.

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33

Buetow, Dennis E., Houqui Chen, Géza Erdő, and Lee S. H. Yi. "Regulation and expression of the multigene family coding light-harvesting chlorophyll a/b-binding proteins of photosystem II." Photosynthesis Research 18, no. 1-2 (October 1988): 61–97. http://dx.doi.org/10.1007/bf00042980.

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34

Heddad, M., and I. Adamska. "Light stress-regulated two-helix proteins in Arabidopsis thaliana related to the chlorophyll a/b-binding gene family." Proceedings of the National Academy of Sciences 97, no. 7 (March 28, 2000): 3741–46. http://dx.doi.org/10.1073/pnas.97.7.3741.

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35

Ganeteg, Ulrika, Åsa Strand, Petter Gustafsson, and Stefan Jansson. "The Properties of the Chlorophyll a/b-Binding Proteins Lhca2 and Lhca3 Studied in Vivo Using Antisense Inhibition." Plant Physiology 127, no. 1 (September 1, 2001): 150–58. http://dx.doi.org/10.1104/pp.127.1.150.

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36

Schwartz, Egbert, and Eran Pichersky. "Sequence of two tomato nuclear genes encoding chlorophyll a/b-binding proteins of CP24, a PSII antenna component." Plant Molecular Biology 15, no. 1 (July 1990): 157–60. http://dx.doi.org/10.1007/bf00017734.

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37

Yan, Ming, and Zhaohe Yuan. "Genome-wide analysis of the family of light-harvesting chlorophyll a/b-binding proteins in pomegranate (Punica granatum L.)." Acta Horticulturae, no. 1297 (November 2020): 647–52. http://dx.doi.org/10.17660/actahortic.2020.1297.85.

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38

Piechulla, Birgit, and Sabine Riesselmann. "Effect of Temperature Alterations on the Diurnal Expression Pattern of the Chlorophyll a/b Binding Proteins in Tomato Seedlings." Plant Physiology 94, no. 4 (December 1, 1990): 1903–6. http://dx.doi.org/10.1104/pp.94.4.1903.

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39

Rikin, A., and S. D. Schwartzbach. "Extremely large and slowly processed precursors to the Euglena light-harvesting chlorophyll a/b binding proteins of photosystem II." Proceedings of the National Academy of Sciences 85, no. 14 (July 1, 1988): 5117–21. http://dx.doi.org/10.1073/pnas.85.14.5117.

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40

Pietrzykowska, M., M. Suorsa, D. A. Semchonok, M. Tikkanen, E. J. Boekema, E. M. Aro, and S. Jansson. "The Light-Harvesting Chlorophyll a/b Binding Proteins Lhcb1 and Lhcb2 Play Complementary Roles during State Transitions in Arabidopsis." Plant Cell 26, no. 9 (September 1, 2014): 3646–60. http://dx.doi.org/10.1105/tpc.114.127373.

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41

Jahns, Peter, and Wolfgang Junge. "ANOTHER ROLE OF CHLOROPHYLL a/b BINDING PROTEINS OF HIGHER PLANTS: THEY MODULATE PROTOLYTIC REACTIONS ASSOCIATED WITH PHOTOSYSTEM II." Photochemistry and Photobiology 57, no. 1 (January 1993): 120–24. http://dx.doi.org/10.1111/j.1751-1097.1993.tb02266.x.

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42

Walling, L. L., Y. C. Chang, D. S. Demmin, and F. M. Holzer. "Isolation, characterization and evolutionary retatedness of three members from the soybean multigene family encoding chlorophyll a/b binding proteins." Nucleic Acids Research 16, no. 22 (November 25, 1988): 10477–92. http://dx.doi.org/10.1093/nar/16.22.10477.

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43

Promnares, Kamoltip, Josef Komenda, Ladislav Bumba, Jana Nebesarova, Frantisek Vacha, and Martin Tichy. "Cyanobacterial Small Chlorophyll-binding Protein ScpD (HliB) Is Located on the Periphery of Photosystem II in the Vicinity of PsbH and CP47 Subunits." Journal of Biological Chemistry 281, no. 43 (August 21, 2006): 32705–13. http://dx.doi.org/10.1074/jbc.m606360200.

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Abstract:

Cyanobacteria contain several genes coding for small one-helix proteins called SCPs or HLIPs with significant sequence similarity to chlorophyll a/b-binding proteins. To localize one of these proteins, ScpD, in the cells of the cyanobacterium Synechocystis sp. PCC 6803, we constructed several mutants in which ScpD was expressed as a His-tagged protein (ScpDHis). Using two-dimensional native-SDS electrophoresis of thylakoid membranes or isolated Photosystem II (PSII), we determined that after high-light treatment most of the ScpDHis protein in a cell is associated with PSII. The ScpDHis protein was present in both monomeric and dimeric PSII core complexes and also in the core subcomplex lacking CP43. However, the association with PSII was abolished in the mutant lacking the PSII subunit PsbH. In a PSII mutant lacking cytochrome b559, which does not accumulate PSII, ScpDHis is associated with CP47. The interaction of ScpDHis with PsbH and CP47 was further confirmed by electron microscopy of PSII labeled with Ni-NTA Nanogold. Single particle image analysis identified the location of the labeled ScpDHis at the periphery of the PSII core complex in the vicinity of the PsbH and CP47. Because of the fact that ScpDHis did not form any large structures bound to PSII and because of its accumulation in PSII subcomplexes containing CP47 and PsbH we suggest that ScpD is involved in a process of PSII assembly/repair during the turnover of pigment-binding proteins, particularly CP47.

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Sullivan, Michael L., and Sharon L. Thoma. "Cloning, molecular characterization, and expression analysis of several red clover cDNAs." Canadian Journal of Plant Science 86, no. 2 (May 5, 2006): 465–68. http://dx.doi.org/10.4141/p05-045.

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To begin gathering information regarding nucleotide sequence similarity between red clover genes and other plant species, especially the model legume Medicago truncatula, several random red clover cDNAs were sequenced. The analyzed cDNAs included genes encoding actin; several proteins involved in photosynthesis including PsaH, PsbR, PsbX, early light-induced protein (ELIP), ferredoxin, chlorophyll a/b binding protein; fructose-bisphosphate aldolase;chloroplastic superoxide dismutase; and GTP-binding protein typA. The gene set had a median sequence identity of 92% with their counterparts from M. truncatula, suggesting its available genomics tools can be applied to red clover. An expression analysis of the gene set in various red clover tissues indicates the genes show a wide range of expression patterns. Consequently, this set of cDNAs and associated data are proving useful as controls in molecular genetic experiments involving red clover. Key words: Red clover, Trifolium pratense, Medicago truncatula, forage legume, genomics, inquiry-based learning

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45

Tanz, Sandra K., Joachim Kilian, Christoffer Johnsson, Klaus Apel, Ian Small, Klaus Harter, Dierk Wanke, Barry Pogson, and Verónica Albrecht. "The SCO2 protein disulphide isomerase is required for thylakoid biogenesis and interacts with LCHB1 chlorophyll a/b binding proteins which affects chlorophyll biosynthesis in Arabidopsis seedlings." Plant Journal 69, no. 5 (December 2, 2011): 743–54. http://dx.doi.org/10.1111/j.1365-313x.2011.04833.x.

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46

Falk, Sebastian, and Irmgard Sinning. "cpSRP43 Is a Novel Chaperone Specific for Light-harvesting Chlorophylla,b-binding Proteins." Journal of Biological Chemistry 285, no. 28 (May 24, 2010): 21655–61. http://dx.doi.org/10.1074/jbc.c110.132746.

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47

Lin, Weiwei, Xiaodong Guo, Xinfeng Pan, and Zhaowei Li. "Chlorophyll Composition, Chlorophyll Fluorescence, and Grain Yield Change in esl Mutant Rice." International Journal of Molecular Sciences 19, no. 10 (September 27, 2018): 2945. http://dx.doi.org/10.3390/ijms19102945.

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To evaluate the effect of changes in chlorophyll (Chl) composition and fluorescence on final yield formation, early senescence leaf (esl) mutant rice and its wild-type cultivar were employed to investigate the genotype-dependent differences in Chl composition, Chl fluorescence, and yield characteristics during the grain-filling stage. However, the temporal expression patterns of key genes involved in the photosystem II (PSII) reaction center in the leaves of two rice genotypes were analyzed by quantitative real-time polymerase chain reaction (qRT-PCR). Results showed that the seed-setting rate, 1000-grain weight, and yield per plant remarkably decreased, and the increase in the 1000-grain weight during the grain-filling stage was retarded in esl mutant rice. Chl composition, maximal fluorescence yield (Fm), variable fluorescence (Fv), a maximal quantum yield of PSII photochemistry (Fv/Fm), and net photosynthetic rate (Pn) in esl mutant rice considerably decreased, thereby indicating the weakened abilities of light energy harvesting and transferring in senescent leaves. The esl mutant rice showed an increase in the minimal fluorescence yield (F0) and 1 − Fv/Fm and decreases in the expression levels of light-harvesting Chl a/b binding protein (Cab) and photosystem II binding protein A (PsbA), PsbB, PsbC, and PsbD encoding for the reaction center of the PSII complex during the grain-filling stage. These results indicated the PSII reaction centers were severely damaged in the mesophyll cells of senescent leaves, which resulted in the weakened harvesting quantum photon and transferring light energy to PSI and PSII for carbon dioxide assimilation, leading to enhanced heat dissipation of light energy and a decrease in Pn.

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48

Dainese, P., and R. Bassi. "Subunit stoichiometry of the chloroplast photosystem II antenna system and aggregation state of the component chlorophyll a/b binding proteins." Journal of Biological Chemistry 266, no. 13 (May 1991): 8136–42. http://dx.doi.org/10.1016/s0021-9258(18)92952-2.

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49

Huang, L., Z. Adam, and N. E. Hoffman. "Deletion Mutants of Chlorophyll a/b Binding Proteins Are Efficiently Imported into Chloroplasts but Do Not Integrate into Thylakoid Membranes." PLANT PHYSIOLOGY 99, no. 1 (May 1, 1992): 247–55. http://dx.doi.org/10.1104/pp.99.1.247.

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50

Pichersky, Eran, Robert Bernatzky, Steven D. Tanksley, R. Bill Breidenbach, Albert P. Kausch, and Anthony R. Cashmore. "Molecular characterization and genetic mapping of two clusters of genes encoding chlorophyll a/b-binding proteins in Lycopersicon esculentum (tomato)." Gene 40, no. 2-3 (January 1985): 247–58. http://dx.doi.org/10.1016/0378-1119(85)90047-2.

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Journal articles on the topic 'Chlorophyll a/b binding proteins'

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