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Littérature scientifique sur le sujet « Thioredoxin »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 25 mai 2024

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Articles de revues sur le sujet "Thioredoxin"

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Langlotz, Petra, Wolfgang Wagner, and Hartmut Follmann. "Green Algae (Scenedesmus obliquus) Contain Three Thioredoxins of Regular Size." Zeitschrift für Naturforschung C 41, no. 11-12 (December 1, 1986): 979–87. http://dx.doi.org/10.1515/znc-1986-11-1205.

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Abstract A comprehensive thioredoxin profile of Scenedesmus obliquus has been established by chromatography of heat-stable protein extracts on five different ion exchange, gel permeation, and affinity chromatography columns and using three different assay systems including homologous S. obliquus ribonucleotide reductase, chloroplast fructose-bis-phosphatase, and NADP malate dehydrogenase. Four different thioredoxins were purified to homogeneity. Besides the large chloroplast thioredoxin f described previously, the algae contain three proteins of molecular weight 12,000 designated thioredoxin

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Nikkanen, Lauri, Jouni Toivola, Manuel Guinea Diaz, and Eevi Rintamäki. "Chloroplast thioredoxin systems: prospects for improving photosynthesis." Philosophical Transactions of the Royal Society B: Biological Sciences 372, no. 1730 (August 14, 2017): 20160474. http://dx.doi.org/10.1098/rstb.2016.0474.

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Thioredoxins (TRXs) are protein oxidoreductases that control the structure and function of cellular proteins by cleavage of a disulphide bond between the side chains of two cysteine residues. Oxidized thioredoxins are reactivated by thioredoxin reductases (TR) and a TR-dependent reduction of TRXs is called a thioredoxin system. Thiol-based redox regulation is an especially important mechanism to control chloroplast proteins involved in biogenesis, in regulation of light harvesting and distribution of light energy between photosystems, in photosynthetic carbon fixation and other biosynthetic pa

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Nikkanen, Lauri, and Eevi Rintamäki. "Thioredoxin-dependent regulatory networks in chloroplasts under fluctuating light conditions." Philosophical Transactions of the Royal Society B: Biological Sciences 369, no. 1640 (April 19, 2014): 20130224. http://dx.doi.org/10.1098/rstb.2013.0224.

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Plants have adopted a number of mechanisms to restore redox homeostasis in the chloroplast under fluctuating light conditions in nature. Chloroplast thioredoxin systems are crucial components of this redox network, mediating environmental signals to chloroplast proteins. In the reduced state, thioredoxins control the structure and function of proteins by reducing disulfide bridges in the redox active site of a protein. Subsequently, an oxidized thioredoxin is reduced by a thioredoxin reductase, the two enzymes together forming a thioredoxin system. Plant chloroplasts have versatile thioredoxin

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Cadet, F., and J. C. Meunier. "Spinach (Spinacia oleracea) chloroplast sedoheptulose-1,7-bisphosphatase. Activation and deactivation, and immunological relationship to fructose-1,6-bisphosphatase." Biochemical Journal 253, no. 1 (July 1, 1988): 243–48. http://dx.doi.org/10.1042/bj2530243.

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In this paper we study activation by dithiothreitol and reduced thioredoxins and deactivation by oxidized thioredoxins f of sedoheptulose-1,7-bisphosphatase. The behaviour of the enzyme when chromatographed on a thioredoxin-Sepharose column is also described. The enzyme is autoxidizable upon removal of reducing agents, and is activated when reduced by any of the thioredoxins. This mechanism may allow the regulation of the Calvin cycle upon light-dark and dark-light transitions. The formation of a stable complex between enzyme and thioredoxin could explain the inhibitory effect of high thioredo

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SERRATO, Antonio J., Juan M. PÉREZ-RUIZ, and Francisco J. CEJUDO. "Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase–thioredoxin h system from wheat." Biochemical Journal 367, no. 2 (October 15, 2002): 491–97. http://dx.doi.org/10.1042/bj20020103.

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Thioredoxins h are ubiquitous proteins reduced by NADPH— thioredoxin reductase (NTR). They are able to reduce disulphides in target proteins. In monocots, thioredoxins h accumulate at high level in seeds and show a predominant localization in the nucleus of seed cells. These results suggest that the NTR—thioredoxin h system probably plays an important role in seed physiology. To date, the study of this system in monocots is limited by the lack of information about NTR. In the present study, we describe the cloning of a full-length cDNA encoding NTR from wheat (Triticum aestivum). The polypepti

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Langlotz, Petra, Wolfgang Wagner, and Hartmut Follmann. "A Large Chloroplast Thioredoxin ƒ Found in Green Algae." Zeitschrift für Naturforschung C 41, no. 3 (March 1, 1986): 275–83. http://dx.doi.org/10.1515/znc-1986-0306.

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Unicellular green algae differ from plant leaves in their thioredoxin profile. Besides several thioredoxins of regular size (Mr = 12,000), the heat-stable protein fraction of extracts from Scenedesmus obliquus cells contains a large protein of molecular weight Mr - 28,000 which is designated thioredoxin ƒ on the basis of typical properties, in particular by its capacity to stimulate spinach chloroplast fructose-bis-phosphatase and, to lower degree, E. coli ribonucleotide reductase. The new thioredoxin was purified to apparent homogeneity by chromatography on DEAE cellulose, Sephadex G-50. CM c

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Bodenstein, Johanna, and Hartmut Follmann. "Characterization of Two Thioredoxins in Pig Heart Including a New Mitochondrial Protein." Zeitschrift für Naturforschung C 46, no. 3-4 (April 1, 1991): 270–79. http://dx.doi.org/10.1515/znc-1991-3-418.

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Heart tissue contains two different thioredoxins. One is a specific mitochondrial protein and is best prepared from pre-isolated, intact heart mitochondria (mt-thioredoxin) whereas mitochondria-depleted tissue homogenates contain the major cellular thioredoxin of cytoplasmic origin (c-thioredoxin). Both heat-stable proteins are clearly differentiated chrom atographically. They exhibit slightly different molecular weights (12300 vs. 12000) and isoelectric points (4.7 vs. 4.8) but differ remarkably in their cysteine content: mt-Thioredoxin has two cysteine residues like the bacterial proteins, a

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Berndt, Carsten, Christopher Horst Lillig, and Arne Holmgren. "Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 3 (March 2007): H1227—H1236. http://dx.doi.org/10.1152/ajpheart.01162.2006.

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Reactive oxygen species (ROS) and the cellular thiol redox state are crucial mediators of multiple cell processes like growth, differentiation, and apoptosis. Excessive ROS production or oxidative stress is associated with several diseases, including cardiovascular disorders like ischemia-reperfusion. To prevent ROS-induced disorders, the heart is equipped with effective antioxidant systems. Key players in defense against oxidative stress are members of the thioredoxin-fold family of proteins. Of these, thioredoxins and glutaredoxins maintain a reduced intracellular redox state in mammalian ce

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Léveillard, Thierry, and Najate Aït-Ali. "Cell Signaling with Extracellular Thioredoxin and Thioredoxin-Like Proteins: Insight into Their Mechanisms of Action." Oxidative Medicine and Cellular Longevity 2017 (2017): 1–11. http://dx.doi.org/10.1155/2017/8475125.

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Thioredoxins are small thiol-oxidoreductase enzymes that control cellular redox homeostasis. Paradoxically, human thioredoxin (TXN1) was first identified as the adult T cell leukemia-derived factor (ADF), a secreted protein. ADF has been implicated in a wide variety of cell-to-cell communication systems acting as a cytokine or a chemokine. TRX80 is a truncated TXN1 protein with cytokine activity. The unconventional secretion mechanism of these extracellular thioredoxins is unknown. The thioredoxin system is relying on glucose metabolism through the pentose phosphate pathway that provides reduc

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Langlotz, Petra, and Hartmut Follmann. "Notes: Formation of Large Thioredoxin f Accompanies Chloroplast Development in Scenedesmus obliquus." Zeitschrift für Naturforschung C 42, no. 11-12 (December 1, 1987): 1364–66. http://dx.doi.org/10.1515/znc-1987-11-1241.

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Chloroplast-free mutant cells C-2A′ of the green algae Scenedesmus obliquus lack thioredoxin f, which functions in the light activation of chloroplast enzymes, but do contain the regular thioredoxins I and II. When dark-grown algae are transferred to light, thioredoxin f activity appears rapidly and increases in parallel with photosynthetic activities: however it precedes chlorophyll biosynthesis. The formation of thioredoxin f is inhibited by cydoheximide indicating that it occurs on the cytoplasmic ribosomes, in accord with the lack of thioredoxin genes on the chloroplast genomes.

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Thèses sur le sujet "Thioredoxin"

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Paunescu, Karina. "DNA-Stabilität und Thioredoxin-Thioredoxin-Reduktase im Zellkern." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969680333.

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Osborne, Leisa Jane. "Characterisation of Thioredoxin Dimers: A Biochemical Study." Thesis, Griffith University, 2011. http://hdl.handle.net/10072/365531.

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In addition to the conserved active site cysteines that are responsible for the classical redox activity of thioredoxins (Trx’s), vertebrate Trx’s contain an additional three conserved cysteines at position 62, 69 and 73. These structural cysteines are known to be subjected to a variety of post translational modifications including dimerisation that are believed to contribute to the regulation and diversity of function of vertebrate Trx’s. Reports of the formation of “disulphide linked dimers” have been a long standing observation since the earliest studies on vertebrate Trx’s, however detaile

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Missirlis, Fanis. "Functional characterization of novel thioredoxin reductase and thioredoxin peroxidase in Drosophila." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2002. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/NQ65830.pdf.

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Shah, Fenil. "Thioredoxin and its Target Proteins: Thioredoxin Expression under Different Oxygen Conditions." Thesis, Griffith University, 2011. http://hdl.handle.net/10072/367670.

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Thioredoxin is an antioxidant protein that performs multiple functions in the intracellular and extracellular environment of cells. Thioredoxin is highly expressed in cancer cells, especially more metastatic and aggressive cancers. Previous studies have demonstrated a functional role for thioredoxin in cancer cell invasion, however little information is currently available regarding the role of thioredoxin in the invasive process. In order to perform these and other functions, thioredoxin interacts with several different protein partners. The primary aim of this project was to identify previou

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Gregory, Mary Sarah-Jane, and n/a. "Thioredoxin and Oxidative Stress." Griffith University. School of Health Science, 2004. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20040301.082639.

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The experiments described in this thesis involve the expression and characterisation of recombinant truncated thioredoxin (tTrx) and the potential involvement that thioredoxin (Trx) has in the cellular responses to oxidative stress. Truncated Trx (80 amino acids) was expressed from a plasmid containing the ORF for tTrx that had been introduced into E.coli BL-21(DE3) cells. The protein was initially extracted using a combination of high concentrations of urea, high pH levels, and multiple sonification steps to remove the tTrx from inclusion bodies formed during expression. This procedure pro

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Gregory, Mary Sarah-Jane. "Thioredoxin and Oxidative Stress." Thesis, Griffith University, 2004. http://hdl.handle.net/10072/367183.

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The experiments described in this thesis involve the expression and characterisation of recombinant truncated thioredoxin (tTrx) and the potential involvement that thioredoxin (Trx) has in the cellular responses to oxidative stress. Truncated Trx (80 amino acids) was expressed from a plasmid containing the ORF for tTrx that had been introduced into E.coli BL-21(DE3) cells. The protein was initially extracted using a combination of high concentrations of urea, high pH levels, and multiple sonification steps to remove the tTrx from inclusion bodies formed during expression. This procedure pro

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Björkhem, Bergman Linda. "Thioredoxin reductase and selenium in carcinogenesis and multidrug resistance /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-954-4/.

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Zhong, Liangwei. "Selenium in mammalian thioredoxin reductase /." Stockholm, 2000. http://diss.kib.ki.se/2000/91-628-4243-9/.

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Callister, Matthew Eric James. "Thioredoxin and the inflammatory response." Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.414905.

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Rozell, Björn. "Immunohistochemical studies of the thioredoxin system." Göteborg : Dept. of Histology, University of Göteborg, 1987. http://catalog.hathitrust.org/api/volumes/oclc/17242526.html.

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Livres sur le sujet "Thioredoxin"

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Joelson, Thorleif. Functional studies of bacteriophage T4 thioredoxin. Uppsala: Institutionen fo r molekyla rbiologi, 1988.

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Nikkola, Matti J. Structural and functional studies on glutaredoxin and thioredoxin. Uppsala: Swedish University of Agricultural Sciences, Dept. of Molecular Biology, 1991.

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Arne, Holmgren, and Karolinska Institute Nobel Conference on Thioredoxin and Glutaredoxin Systems: Structure and Function (1985 : Södergarn, Sweden), eds. Thioredoxin and glutaredoxin systems: Structure and function. New York: Raven Press, 1986.

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Häberlein, Ingo. Charakterisierung der Thioredoxine und deren Zielsysteme in der Sojabohne (Glycine max). Gauting bei München: A.S. und Ch. C. Intemann, 1987.

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1942-, Sies H., and Packer Lester, eds. Protein sensors and reactive oxygen species. San Diego, Calif: Academic Press, 2002.

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English, Shane. The cloning and characterization of the cDNA encoding mouse gamma-glutamyl cysteine synthetase and thioredoxin. Sudbury, Ont: Laurentian University, 2001.

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Lester, Packer, ed. Biothiols. San Diego: Academic Press, 1995.

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service), ScienceDirect (Online, ed. Thiol redox transitions in cell signaling: Cellular localization and signaling. San Diego, Calif: Elsevier, 2010.

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Thioredoxin and Glutaredoxin Systems. MDPI, 2019. http://dx.doi.org/10.3390/books978-3-03897-837-4.

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Holmgren, Arne. Thioredoxin and Glutaredoxin Systems: Structure and Function. Raven Pr, 1986.

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Chapitres de livres sur le sujet "Thioredoxin"

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Didier, C., M. J. Richard, J. C. Beani, and A. Favier. "Thioredoxin/Thioredoxin Reductase System." In Trace Elements in Man and Animals 10, 143. New York, NY: Springer US, 2002. http://dx.doi.org/10.1007/0-306-47466-2_36.

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Saccoccia, Fulvio, and Andrea Bellelli. "Thioredoxin Reductase." In Encyclopedia of Signaling Molecules, 5385–99. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101928.

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Hanschmann, Eva-Maria, and Carsten Berndt. "Thioredoxin (TXN)." In Encyclopedia of Signaling Molecules, 5377–85. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101939.

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Arnér, Elias S. J., and Arne Holmgren. "Thioredoxin System." In Encyclopedia of Cancer, 1–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_5777-3.

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Huang, Jin, and Liangwei Zhong. "Thioredoxin Reductase." In Advanced Topics in Science and Technology in China, 41–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_3.

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Saccoccia, Fulvio, and Andrea Bellelli. "Thioredoxin Reductase." In Encyclopedia of Signaling Molecules, 1–15. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101928-1.

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Hanschmann, Eva-Maria, and Carsten Berndt. "Thioredoxin (TXN)." In Encyclopedia of Signaling Molecules, 1–9. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101939-1.

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Arnér, Elias S. J., and Arne Holmgren. "Thioredoxin System." In Encyclopedia of Cancer, 4508–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_5777.

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Arnér, Elias S. J., and Arne Holmgren. "Thioredoxin System." In Encyclopedia of Cancer, 3670–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5777.

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Schomburg, D., M. Salzmann, and D. Stephan. "Thioredoxin reductase (NADPH)." In Enzyme Handbook 7, 267–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_53.

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Actes de conférences sur le sujet "Thioredoxin"

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Branković, Jovica, Vesna Milovanović, Zorica D. Petrović, and Vladimir P. Petrović. "GALLIC ACID HYDRAZONES: ‘IN SILICO’ INHIBITION OF THIOREDOXIN REDUCTASE." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.320b.

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Gallic hydrazones, as gallic acid derivatives, are known as pharmacophores of numerous multipotent agents. Among them, antiproliferative activity is one of the most important. On the other hand, thioredoxin reductase (TrxR1) is a part of the thioredoxin system, one of the most important systems responsible for maintaining the redox equilibrium inside the cell. It is overexpressed in different forms of tumors. Bearing this in mind, TrxR1 is a valid target for the development of compounds with potential antiproliferative activity. For this purpose, eight gallic acid-based hydrazones are selected

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Vitiello, Peter, and Elliot Bloom. "Hyperoxic Modification Of Thioredoxin-Dependent Pathways." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5960.

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Vitiello, P., C. Aegerter, J. Hoffman, B. Mordhorst, A. Fairchild, B. Forred, and T. E. Tipple. "Impairment of Thioredoxin 1 Disrupts Perinatal Alveolar Development." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a6043.

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Hu, H., L. Lu, E. Block, and JM Patel. "Priming Donor Lungs with Thioredoxin Attenuates Allograft Rejection." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5684.

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Vitiello, P., Y. Cao, C. Esslinger, C. Aegerter, K. Bruening, J. Hoffman, T. E. Tipple, and B. Forred. "Hyperoxic Inhibition of Thioredoxin 1 Activity Disrupts Perinatal Alveologenesis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6394.

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Leaver, Susannah K., Gregory Quinlan, Timothy W. Evans, and Anne Burke-Gaffney. "TNF ± MODIFIES THIOREDOXIN-INDUCED CYTOKINE RELEASE FROM HUMAN MONOCYTES." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6150.

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Nikitjuka, Anna, and Raivis Žalubovskis. "Natural-like scaffolds targeting thioredoxin reductase for anticancer therapy." In 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11458.

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Ito, W., N. Kobayashi, M. Takeda, T. Tanigai, Y. Yamada, S. Ueki, H. Nakamura, H. Kayaba, J. Yodoi, and J. Chihara. "Thioredoxin Reduces C-C Chemokine-Induced Chemotaxis of Human Eosinophils." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1340.

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Rogozin, E. "Biotechnology for production of recombinant hybrid proteins from plants and microbes with antifungal activity." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.206.

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The principle of obtaining recombinant antimicrobial polypeptides from plant and microbial origins as a part of chimeric proteins with thioredoxin by heterologous expression in a prokaryotic system is presented. The results obtained in terms of their antifungal activity in relation to plant pathogenic micromycetes allow us to consider these compounds as prototypes of some active substances of environmentally friendly biofungicides, as well as possible components of hybrid plant protection products against fungal diseases.

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Grandjean, Geoffrey, Geoffrey Bartholomeusz, John Kingston та Garth Powis. "Abstract 2188: A high throughput RNAi screen for regulators of thioredoxin in pancreatic cancer cells identifies components of TGFβ-signaling as inducers of thioredoxin expression". У Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2188.

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Rapports d'organisations sur le sujet "Thioredoxin"

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Lazo, John S. Novel Thioredoxin Inhibitors for Breast Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada396648.

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Lazo, John S. Novel Thioredoxin Inhibitors for Breast Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada409411.

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Porter, M. A., and F. C. Hartman. Thioredoxin binding site of phosphoribulokinase overlaps the catalytic site. [R]. Office of Scientific and Technical Information (OSTI), January 1986. http://dx.doi.org/10.2172/5463659.

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Chuck, Steven L. The Non-Classical Secretion of Thioredoxin from Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada407677.

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Chuck, Steven L. The Non-Classical Secretion of Thioredoxin from Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, June 2004. http://dx.doi.org/10.21236/ada426431.

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Collier, Jackie, L. A Novel, Photosynthesis-Associated Thioredoxin-Like Gene: Final Technical Report. Office of Scientific and Technical Information (OSTI), September 2005. http://dx.doi.org/10.2172/850272.

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Chuck, Steven L. The Non-Classical Secretion of Thioredoxin from Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada425885.

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Cassidy, Pamela. Covalent Adducts Between Thioredoxin Reductase and Endogenous Electrophiles in Human Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2005. http://dx.doi.org/10.21236/ada446694.

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Vargas Castro, José Livan, and MariCruz González García. Analysis of Regulatory Elements Related to Cytokinins and Interactions with Microorganisms in Promoters of Thioredoxins and Glutaredoxins. Fundación Avanza, May 2024. http://dx.doi.org/10.60096/fundacionavanza/8642024.

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Análisis in silico de elementos reguladores de promotores de tiorredoxinas y glutarredoxinas para ver si estas proteínas pueden ser reguladas por citoquininas y elementos de interacción planta-microorganismos.

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Christopher, David A., and Avihai Danon. Plant Adaptation to Light Stress: Genetic Regulatory Mechanisms. United States Department of Agriculture, May 2004. http://dx.doi.org/10.32747/2004.7586534.bard.

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Original Objectives: 1. Purify and biochemically characterize RB60 orthologs in higher plant chloroplasts; 2. Clone the gene(s) encoding plant RB60 orthologs and determine their structure and expression; 3. Manipulate the expression of RB60; 4. Assay the effects of altered RB60 expression on thylakoid biogenesis and photosynthetic function in plants exposed to different light conditions. In addition, we also examined the gene structure and expression of RB60 orthologs in the non-vascular plant, Physcomitrella patens and cloned the poly(A)-binding protein orthologue (43 kDa RB47-like protein).

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