DOCSLIB.ORG

Occurrence, Biosynthesis and Function of Isoprenoid Quinones

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Occurrence, Biosynthesis and Function of Isoprenoid Quinones View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1797 (2010) 1587–1605 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbabio Review Occurrence, biosynthesis and function of isoprenoid quinones Beatrycze Nowicka, Jerzy Kruk ⁎ Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland article info abstract Article history: Isoprenoid quinones are one of the most important groups of compounds occurring in membranes of living Received 13 April 2010 organisms. These compounds are composed of a hydrophilic head group and an apolar isoprenoid side chain, Received in revised form 9 June 2010 giving the molecules a lipid-soluble character. Isoprenoid quinones function mainly as electron and proton Accepted 14 June 2010 carriers in photosynthetic and respiratory electron transport chains and these compounds show also Available online 19 June 2010 additional functions, such as antioxidant function. Most of naturally occurring isoprenoid quinones belong to naphthoquinones or evolutionary younger benzoquinones. Among benzoquinones, the most widespread and Keywords: Biosynthesis important are ubiquinones and plastoquinones. Menaquinones, belonging to naphthoquinones, function in Electron transport chain respiratory and photosynthetic electron transport chains of bacteria. Phylloquinone K1,aphytyl Isoprenoid quinone naphthoquinone, functions in the photosynthetic electron transport in photosystem I. Ubiquinones Naphthoquinone participate in respiratory chains of eukaryotic mitochondria and some bacteria. Plastoquinones are Plastoquinone components of photosynthetic electron transport chains of cyanobacteria and plant chloroplasts. Ubiquinone Biosynthetic pathway of isoprenoid quinones has been described, as well as their additional, recently recognized, diverse functions in bacterial, plant and animal metabolism. © 2010 Elsevier B.V. All rights reserved. 1. Introduction quinones is more polar and the quinol head group is thought to preferentially localize in polar, interphase region of membranes [3,4]. Isoprenoid quinones are membrane-bound compounds found in The ability of reversible reduction and the presence of the lipid- nearly all living organisms. The only exception presently known is soluble side chain make the isoprenoid quinones ideal candidates for some obligatory fermentative bacteria that lost the ability of synthesis their function as hydrogen shuttles between different protein of isoprenoid quinones [1] and methanogenic Archea, belonging to complexes of biological membranes. Isoprenoid quinones, which are Methanosarcinales [2]. Isoprenoid quinones are composed of a polar also termed prenylquinones [5,6], function in electron transport head group and a hydrophobic side chain. The apolar isoprenoid side chains as membrane-bound, mobile hydrogen carriers but some of chain gives the molecules a lipid-soluble character and anchors them these molecules are permanently associated with proteins and par- in membrane lipid bilayers, whereas the hydrophilic head group ticipate in electron transport within protein complexes. Such protein- enables interaction with hydrophilic parts of proteins. It is generally bound prenylquinones, where semiquinone form is stabilized, often accepted that long-chain, isoprenoid quinones localize in the hydro- act as a “gates” between one and two-electron processes. The reduced phobic mid-plane region of the lipid bilayer, whereas the polar head forms of isoprenoid quinones have pronounced antioxidant proper- can oscillate between mid-plane and polar interphase of the mem- ties and protect membranes from lipid peroxidation and deleterious brane [3]. The quinone ring can undergo two-step reversible reduc- effects of reactive oxygen species on membrane components. During tion leading to quinol form (Fig. 1). The reduced form of isoprenoid recent years, a vast number of data concerning function of isoprenoid quinones as enzyme cofactors accumulated. These compounds were also postulated to participate in regulation of gene expression and Abbreviations: DHFL, dehypoxanthinylfutalosine; DHNA, 1,4-dihydroxy-2- signal transduction within cells [7]. naphthoate; DMK, demethylmenaquinone; DXP, 1-deoxy-D-xylulose-5-phosphate; The great majority of biological isoprenoid quinones belong to fl + ETF-QU, electron transfer avoprotein:UQ oxidoreductase; FNR, ferredoxin:NADP naphthoquinones or benzoquinones. The two most important groups oxidoreductase; GGCX, γ-glutamyl carboxylase; Gla, γ-carboxyglutamate; HGA, of benzoquinones are ubiquinones and plastoquinones, differing in homogentisate; K1, phylloquinone; MK, menaquinone; MKH2, menaquinol; MTQ, methionaquinone; MVA, mevalonate; NDH-2, type II dehydrogenase; PHB, p-hydro- the pattern of ring substitution. Besides, the hydrophobic side chains xybenzoate; PS, photosystem; PQ, plastoquinone; PQH2, plastoquinol; QFR, quinol: of isoprenoid quinones can vary not only in the length but also in a fumarate oxidoreductase; ROS, reactive oxygen species; RQ, rhodoquinone; RQH2, degree of saturation, as well as in the presence of additional groups. rhodoquinol; SQR, sulfide:quinone oxidoreductase; TPQ, thermoplasmaquinone; TQ, Different groups of isoprenoid quinones occur in different taxonomic tocopherol quinone; TQH , tocopherol quinol; UQ, ubiquinone; UQH , ubiquinol 2 2 fi ⁎ Corresponding author. groups of organisms, making isoprenoid quinone pro le a useful E-mail address: [email protected] (J. Kruk). taxonomic tool [1]. 0005-2728/$ – see front matter © 2010 Elsevier B.V. All rights reserved. doi:10.1016/j.bbabio.2010.06.007 1588 B. Nowicka, J. Kruk / Biochimica et Biophysica Acta 1797 (2010) 1587–1605 –· Fig. 1. Redox reactions of the quinone ring, Q—oxidized form, Q —charged, semiquinone radical, unstable, can be stabilized by interaction with proteins, QH2—stable, non-charged hydroquinone form. 2. Isoprenoid naphthoquinones mentioned, that some obligatory fermentative bacteria had lost the ability to synthesize menaquinones—most of bacteria of genus 2.1. Menaquinones and related compounds Lactobacillus and Streptococcus, but genes of menaquinone biosyn- thetic pathway can be found in some of the species [1,12]. The 2.1.1. Occurrence isoprenoid side chain of menaquinones is most frequently composed Menaquinones (MK) (Fig. 2) are the most widespread microbial of 6–10 prenyl units but also homologues with one to 14 prenyl units respiratory quinones that are evolutionary most ancient type of were found in some species [1]. The side chain is most often fully isoprenoid quinones [8]. These compounds can be found in many unsaturated, but it can be also partially or fully saturated in some groups of Archaea [9] and bacteria, such as γ- δ- ε-proteobacteria, organisms [1]. The length and degree of saturation of the side chain gram-positive bacteria, green sulfur bacteria, green filamentous are often dependent on the growth temperature of a given species. bacteria, deinococci and flavobacteria [8,10,11]. Menaquinones have Menaquinones contain methyl-naphthoquinone as a head group, but low midpoint redox potential, and their appearance in early phase of in some prokaryotes compounds with different modifications of evolution can be connected with the reducing character of atmo- the head group were identified (Fig. 2). Among the Archea, ther- sphere before appearance of oxygenic photosynthesis and the moplasmaquinone (TPQ) and methionaquinone (MTQ) occur in following increase in oxygen concentration in the environment. The Thermoplasma [9,13]. Demethylmenaquinones (DMKs) and methyl- “transition” from naphthoquinones to other quinones, showing menaquinones are often used by proteobacteria and gram-positive higher midpoint redox potential, occurred independently in a few bacteria [1,14]. Chlorobiumquinone (1′-oxo-menaquinone-7) was groups of Prokaryota as an adaptation to aerobic metabolism. The found in photosynthetic green sulfur bacteria—it is only known reduced menaquinones become rapidly and noncatalytically oxidized isoprenoid naphthoquinone containing carbonyl group in the side in the presence of oxygen [11], therefore these compounds cannot chain [1]. Surprisingly, chlorobiumquinone was also identified as a efficiently operate in an atmosphere containing oxygen. It should be major isoprenoid quinone in parasitic protozoan Leischmania Fig. 2. Isoprenoid naphthoquinones: MK-8, menaquinone-8 and DMK-8, demethylmenaquinone-8 present in E. coli; TPQ-7, thermoplasmaquinone-7 and MTQ-7, methionaquinone- 7 found in Thermoplasma acidophilum; ChQ, chlorobiumquinone (1′-oxo-menaquinone-7) occurring in Chlorobium tepidum, PhQ—phylloquinone. B. Nowicka, J. Kruk / Biochimica et Biophysica Acta 1797 (2010) 1587–1605 1589 donovani [15]. It is thought to act in plasma membrane of the parasite of certain men genes. After extensive studies including bioinformatic as a part of defense system against oxidative burst of the host. analysis, mutagenesis, radioisotope labeling and genetic engineering, Moreover, the presence of homologues of the genes found in the alternative, so called “futalosine pathway” has been identified photosynthetic bacteria was discovered in trypanosomatids, which (Fig. 3B) [22]. In this pathway, four enzymes are engaged in DHNA let to hypothesize that ancestors of Leishmania could have had biosynthesis: MqnA
Load more

Recommended publications
  • Light-Induced Psba Translation in Plants Is Triggered by Photosystem II Damage Via an Assembly-Linked Autoregulatory Circuit
    Light-induced psbA translation in plants is triggered by photosystem II damage via an assembly-linked autoregulatory circuit Prakitchai Chotewutmontria and Alice Barkana,1 aInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403 Edited by Krishna K. Niyogi, University of California, Berkeley, CA, and approved July 22, 2020 (received for review April 26, 2020) The D1 reaction center protein of photosystem II (PSII) is subject to mRNA to provide D1 for PSII repair remain obscure (13, 14). light-induced damage. Degradation of damaged D1 and its re- The consensus view in recent years has been that psbA transla- placement by nascent D1 are at the heart of a PSII repair cycle, tion for PSII repair is regulated at the elongation step (7, 15–17), without which photosynthesis is inhibited. In mature plant chloro- a view that arises primarily from experiments with the green alga plasts, light stimulates the recruitment of ribosomes specifically to Chlamydomonas reinhardtii (Chlamydomonas) (18). However, we psbA mRNA to provide nascent D1 for PSII repair and also triggers showed recently that regulated translation initiation makes a a global increase in translation elongation rate. The light-induced large contribution in plants (19). These experiments used ribo- signals that initiate these responses are unclear. We present action some profiling (ribo-seq) to monitor ribosome occupancy on spectrum and genetic data indicating that the light-induced re- cruitment of ribosomes to psbA mRNA is triggered by D1 photo- chloroplast open reading frames (ORFs) in maize and Arabi- damage, whereas the global stimulation of translation elongation dopsis upon shifting seedlings harboring mature chloroplasts is triggered by photosynthetic electron transport.
    [Show full text]
  • Greencut Protein CPLD49 of Chlamydomonas Reinhardtii Associates with Thylakoid Membranes and Is Required for Cytochrome B6f Complex Accumulation
    The Plant Journal (2018) 94, 1023–1037 doi: 10.1111/tpj.13915 GreenCut protein CPLD49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b6f complex accumulation Tyler M. Wittkopp1,2,† , Shai Saroussi2,† , Wenqiang Yang2 , Xenie Johnson3 , Rick G. Kim1,2 , Mark L. Heinnickel2, James J. Russell1, Witchukorn Phuthong4 , Rachel M. Dent5,6 , Corey D. Broeckling7 , Graham Peers8 , Martin Lohr9 , Francis-Andre Wollman10 , Krishna K. Niyogi5,6 and Arthur R. Grossman2,* 1Department of Biology, Stanford University, Stanford, CA 94305, USA, 2Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA, 3Laboratoire de Bioenerg etique et Biotechnologie des Bacteries et Microalgues, CEA Cadarache, Saint Paul lez Durance, France, 4Department of Materials Science and Engineering, Stanford University, Stanford, CA 94305, USA, 5Department of Plant and Microbial Biology, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720- 3102, USA, 6Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA, 7Proteomics and Metabolomics Facility, Colorado State University, Fort Collins, CO 80523, USA, 8Department of Biology, Colorado State University, Fort Collins, CO 80523, USA, 9Institut fur€ Molekulare Physiologie – Pflanzenbiochemie, Johannes Gutenberg-Universitat,€ 55099 Mainz, Germany, and 10Institut de Biologie Physico-Chimique, CNRS-UPMC, Paris, France Received 27 October 2017; revised 23 February 2018; accepted 6 March 2018; published online 30 March 2018. *For correspondence (e-mail [email protected]). †These authors contributed equally to this work. SUMMARY The GreenCut encompasses a suite of nucleus-encoded proteins with orthologs among green lineage organ- isms (plants, green algae), but that are absent or poorly conserved in non-photosynthetic/heterotrophic organisms.
    [Show full text]
  • Structure of the Cytochrome B6 F Complex of Oxygenic Photosynthesis
    Structure of the Cytochrome b6 f Complex of Oxygenic Photosynthesis The photosynthetic unit of oxygenic photosynthesis data of 3.0 Å from the complex crystal with another is organized as two large multimolecular membrane analogue inhibitor, TDS, was collected at the SBC complexes, photosystem II (PSII) that extracts low- beamline 19ID, APS. The initial model was developed energy electrons from water and photosystem I (PSI) into a 3.4 Å map of the native complex. Final that raises the energy level of such electrons using refinement was carried out with a dataset from a co- light energy to produce a strong reductant, NADPH. crystal with TDS (Figs. 2, 3). The two photosystems operate in a series linked by a Viewed along the membrane normal, the b6f × third multiprotein complex called the cytochrome b6f complex is 90 Å 55 Å within the membrane side, × complex (Fig.1). The cytochrome b6f complex is a and 120 Å 75 Å on the lumen (p)side (Fig. 2). A membrane-spanning protein complex embedded in prominent feature of this structure is an extended the thylakoid membrane of photosynthetic organisms. quinone exchange cavity between the monomers, The molecular weight of the complex is 220,000 as a which exchanges lipophilic plastoquinone in the dimer with 26 transmembrane helices. The b6f complex bilayer center, and also mediates the electron and controls the electron transfer between the plastoquinol proton transfer across the complex. The heme-binding reduced by PSII and the electron carrier protein 4 transmembrane helices core of the b6f complex plastocyanin that associate with PSI.
    [Show full text]
  • A Defined Protein–Detergent–Lipid Complex for Crystallization Of
    A defined protein–detergent–lipid complex for crystallization of integral membrane proteins: The cytochrome b6f complex of oxygenic photosynthesis Huamin Zhang*, Genji Kurisu†, Janet L. Smith, and William A. Cramer* Department of Biological Sciences, Lilly Hall of Life Sciences, Purdue University, West Lafayette, IN 47907-2054 Communicated by Michael G. Rossmann, Purdue University, West Lafayette, IN, March 12, 2003 (received for review December 18, 2002) The paucity of integral membrane protein structures creates a resulting lability of the IMP (12), crystallization may be frus- major bioinformatics gap, whose origin is the difficulty of crystal- trated. This ‘‘detergent problem’’ is represented in Fig. 1 a and lizing these detergent-solubilized proteins. The problem is partic- b by the ordered arrangement of the transmembrane helices of ularly formidable for hetero-oligomeric integral membrane pro- an oligomeric IMP such as the cyt b6f complex in a lipid bilayer teins, where crystallization is impeded by the heterogeneity and membrane (Fig. 1a), compared with their disordered arrange- instability of the protein subunits and the small lateral pressure ment in a detergent micelle, which is depicted by a splayed imposed by the detergent micelle envelope that surrounds the arrangement of the transmembrane ␣-helices (Fig. 1b). The hydrophobic domain. In studies of the hetero (eight subunit)- spatial- and time-dependent disorder of the detergent micelle (2, dimeric 220,000 molecular weight cytochrome b6f complex, de- 14), described by the heterogeneity of the micelle shown in Fig. rived from the thermophilic cyanobacterium, Mastigocladus lami- 1b, is also an impediment to crystallization. From crystallization nosus, crystals of the complex in an intact state could not be and diffraction studies of a hetero-oligomeric integral mem- obtained from highly purified delipidated complex despite exhaus- brane protein, discussed below, it is proposed that addition of a tive screening.
    [Show full text]
  • Electrophoresis
    ELECTROPHORESIS Supporting Information for Electrophoresis DOI 10.1002/elps.200406079 Michalis Aivaliotis, Carsten Corvey, Irene Tsirogianni, Michael Karas and Georgios Tsiotis Membrane proteome analysis of the green-sulfur bacterium Chlorobium tepidum ã 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim Electrophoresis 2004, 25, 0001±0010 1 6 Addendum Table 1. List of identified proteins separated in 2-D gel with Triton X-100 No. Protein definition Accession Predicted Peptides Peptide TM GRAVYSignalP Aro- Predicted b) No./gene Mr/pI matched coverage a-heli- matic localization (%) cesa) anchor Transport and binding proteins 1 ArsA ATPase family protein Q8KDR5/CT0980 44541/5.0 17 48 1 20.117 ± ± Inner membrane 2 Outer membrane efflux Q8KED1/CT0758 52716/8.9 8 16 3 20.163 ± ± Outer membrane protein, putative 3 ABC transporter, periplasmic Q8KDW4/CT0930 33207/8.9 9 26 3 20.388 YES 1±25 ± Inner membrane substrate-binding protein Energy metabolism 4 ATP synthase F1, a-subunit Q8KAW8/ATPA 56869/6.3 31 50 2 20.051 ± ± Inner membrane 5 ATP synthase, b-chain Q8KAC9/ATPD 50125/5.0 37 77 1 20.130 ± ± Inner membrane 6 ATP synthase F0, B subunit Q8KGE9/ATPF 19437/7.7 8 33 1 20.225 YES 1±39 ± Inner membrane 7 Bacteriochlorophyl A protein Q46393/FMOA 40383/7.1 34 78 ± 20.288 ± ± Inner membrane 8 Chlorosome envelope O68991/GSMH 21779/4.9 7 44 2 20.125 ± ± Chlorosome protein H 9 Chlorosome envelope O68988/GSMI 25911/7.6 11 60 2 0.082 ± ± Chlorosome protein I 10 Chlorosome envelope Q8KEN5/CSMX 23970/5.7 9 40 ± 20.155 ± ± Chlorosome protein X 11 Cytochrome
    [Show full text]
  • Chloroflexus Aurantiacus
    Tang et al. BMC Genomics 2011, 12:334 http://www.biomedcentral.com/1471-2164/12/334 RESEARCHARTICLE Open Access Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus Kuo-Hsiang Tang1, Kerrie Barry2, Olga Chertkov3, Eileen Dalin2, Cliff S Han3, Loren J Hauser4, Barbara M Honchak1, Lauren E Karbach1,7, Miriam L Land4, Alla Lapidus5, Frank W Larimer4, Natalia Mikhailova5, Samuel Pitluck2, Beverly K Pierson6 and Robert E Blankenship1* Abstract Background: Chloroflexus aurantiacus is a thermophilic filamentous anoxygenic phototrophic (FAP) bacterium, and can grow phototrophically under anaerobic conditions or chemotrophically under aerobic and dark conditions. According to 16S rRNA analysis, Chloroflexi species are the earliest branching bacteria capable of photosynthesis, and Cfl. aurantiacus has been long regarded as a key organism to resolve the obscurity of the origin and early evolution of photosynthesis. Cfl. aurantiacus contains a chimeric photosystem that comprises some characters of green sulfur bacteria and purple photosynthetic bacteria, and also has some unique electron transport proteins compared to other photosynthetic bacteria. Methods: The complete genomic sequence of Cfl. aurantiacus has been determined, analyzed and compared to the genomes of other photosynthetic bacteria. Results: Abundant genomic evidence suggests that there have been numerous gene adaptations/replacements in Cfl. aurantiacus to facilitate life under both anaerobic and aerobic conditions, including duplicate genes and gene clusters for the alternative complex III (ACIII), auracyanin and NADH:quinone oxidoreductase; and several aerobic/ anaerobic enzyme pairs in central carbon metabolism and tetrapyrroles and nucleic acids biosynthesis. Overall, genomic information is consistent with a high tolerance for oxygen that has been reported in the growth of Cfl.
    [Show full text]
  • S1 Appendix Supplemental Reference
    S1 Appendix Supplemental reference accompanying Table S4 Adhikari, N.D., Froehlich, J.E., Strand, D.D., Buck, S.M., Kramer, D.M. and Larkin, R.M. (2011) GUN4-porphyrin complexes bind the chlH/GUN5 subunit of Mg-chelatase and promote chlorophyll biosynthesis in Arabidopsis. Plant Cell, 23, 1449–1467. Albee, A.J., Kwan, A.L., Lin, H., Granas, D., Stormo, G.D. and Dutcher, S.K. (2013) Identification of cilia genes that affect cell-cycle progression using whole-genome transcriptome analysis in chlamydomonas reinhardtti. G3 Genes, Genomes, Genet., 3, 979–991. Auchincloss, A.H., Zerges, W., Perron, K., Girard-Bascou, J. and Rochaix, J.D. (2002) Characterization of Tbc2, a nucleus-encoded factor specifically required for translation of the chloroplast psbC mRNA in Chlamydomonas reinhardtii. J. Cell Biol., 157, 953–962. Barneche, F., Winter, V., Crèvecœur, M. and Rochaix, J.D. (2006) ATAB2 is a novel factor in the signalling pathway of light-controlled synthesis of photosystem proteins. EMBO J., 25, 5907–5918. Bellafiore, S., Barneche, F., Peltler, G. and Rochalx, J.D. (2005) State transitions and light adaptation require chloroplast thylakoid protein kinase STN7. Nature, 433, 892–895. Blume, C., Behrens, C., Eubel, H., Braun, H.P. and Peterhansel, C. (2013) A possible role for the chloroplast pyruvate dehydrogenase complex in plant glycolate and glyoxylate metabolism. Phytochemistry, 95, 168–176. Bohne, A.V., Schwarz, C., Schottkowski, M., Lidschreiber, M., Piotrowski, M., Zerges, W. and Nickelsen, J. (2013) Reciprocal Regulation of Protein Synthesis and Carbon Metabolism for Thylakoid Membrane Biogenesis. PLoS Biol., 11. Boulouis, A., Raynaud, C., Bujaldon, S., Aznar, A., Wollman, F.A.
    [Show full text]
  • A Stromal Region of Cytochrome B6f Subunit IV Is Involved in the Activation of the Stt7 Kinase in Chlamydomonas
    A stromal region of cytochrome b6f subunit IV is involved in the activation of the Stt7 kinase in Chlamydomonas Louis Dumasa, Francesca Zitob, Stéphanie Blangya, Pascaline Auroya, Xenie Johnsona, Gilles Peltiera, and Jean Alrica,1 aLaboratoire de Bioénergétique et Biotechnologie des Bactéries et Microalgues, Commissariat à l’Energie Atomique et aux Energies Alternatives (CEA), CNRS, Aix-Marseille Université, UMR 7265, Institut de Biosciences et Biotechnologies d’Aix-Marseille, CEA Cadarache, F-13108 Saint-Paul-lez-Durance, France; and bLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, UMR7099, University Paris Diderot, Sorbonne Paris Cité, Paris Sciences et Lettres Research University, F-75005 Paris, France Edited by Jean-David Rochaix, University of Geneva, Geneva 4, Switzerland, and accepted by Editorial Board Member Joseph R. Ecker September 25, 2017 (received for review July 28, 2017) The cytochrome (cyt) b6f complex and Stt7 kinase regulate the and PQH2 binding are required (10, 17, 18), the PetO subunit of antenna sizes of photosystems I and II through state transitions, cyt b6f is phosphorylated by Stt7 during PQ pool reduction (19), which are mediated by a reversible phosphorylation of light har- and the lumenal domain of Stt7 interacts directly with the vesting complexes II, depending on the redox state of the plasto- Rieske-ISP subunit of cyt b6f and contains two conserved cyste- quinone pool. When the pool is reduced, the cyt b6f activates the ine residues (20). However, the Stt7 kinase domain (20) and Stt7 kinase through a mechanism that is still poorly understood. After Stt7-dependent LHCII phosphorylation sites (21) are located on random mutagenesis of the chloroplast petD gene, coding for subunit the stromal side of the membrane.
    [Show full text]
  • Chromoplast Differentiation in Bell Pepper (Capsicum Annuum) Fruits
    bioRxiv preprint doi: https://doi.org/10.1101/2020.09.29.299313; this version posted September 30, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. RESOURCE Chromoplast differentiation in bell pepper (Capsicum annuum) fruits Anja Rödiger1, 2, Birgit Agne1, 2, Dirk Dobritzsch1, Stefan Helm1, Fränze Müller1, 3, Nina Pötzsch1 and Sacha Baginsky1, 2* 1Plant Biochemistry, Institute of Biochemistry and Biotechnology, Martin-Luther-Universität Halle-Wittenberg, Halle (Saale), Germany 2Biochemistry of Plants, Biology and Biotechnology, Ruhr-University Bochum, Bochum, Germany 3Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Freiburg, Germany Keywords: quantitative proteomics, CN PAGE, plastid differentiation, chromorespiration Running Title: Proteomics of chromoplast differentiation * Correspondence: Sacha Baginsky, Biochemistry of Plants, ND3/126, Universitätsstrasse 150, 44801 Bochum, Germany, Email: [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.09.29.299313; this version posted September 30, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Abstract We report here a detailed analysis of the proteome adjustments that accompany chromoplast differentiation from chloroplasts during bell-pepper fruit ripening. While the two photosystems are disassembled and their constituents degraded, the cytochrome b6f complex, the ATPase complex as well as Calvin cycle enzymes are maintained at high levels up to fully mature chromoplasts.
    [Show full text]
  • Thesis Reference
    Thesis C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization DESMURS-ROUSSEAU, Marjorie Abstract Cette thèse a permis d'identifier C11orf83, désormais appelé UQCC3, comme étant une protéine mitochondriale ancrée dans la membrane interne. Nous avons constaté l'implication de C11orf83 dans l'assemblage du complexe III de la chaîne respiratoire via la stabilisation du complexe intermédiaire MT-CYB/UQCRB/UQCRQ. Nous avons également prouvé que C11orf83 était associée avec le dimère de complexe III et était détectée dans le supercomplexe III2/IV. Son absence induit une baisse significative de ce supercomplexe et du respirasome (I/III2/IV). La capacité de C11orf83 de lier les cardiolipines, connues pour être impliquées dans la formation et la stabilisation de ces supercomplexes, pourrait expliquer ces résultats. Ainsi, ce travail de thèse en lien avec une récente étude clinique mettant en évidence une déficience du complexe III chez un patient atteint d'une mutation du gène C11orf83 (Wanschers et al., 2014) permet d'améliorer les connaissances sur l'assemblage du complexe III et la compréhension d'une maladie mitochondriale. Reference DESMURS-ROUSSEAU, Marjorie. C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization. Thèse de doctorat : Univ. Genève, 2015, no. Sc. 4857 DOI : 10.13097/archive-ouverte/unige:108015 URN : urn:nbn:ch:unige-1080158 Available at: http://archive-ouverte.unige.ch/unige:108015 Disclaimer: layout of this document may differ from the published version. 1 / 1 UNIVERSITÉ DE GENÈVE Département de Biologie Cellulaire FACULTÉ DES SCIENCES Professeur Jean-Claude Martinou Département de Science des Protéines Humaines FACULTÉ DE MEDECINE Professeur Amos Bairoch C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization.
    [Show full text]
  • Time-Independent Structure of the Cytochrome B6f Complex† William A
    Evolution of Photosynthesis: Time-Independent Structure of the Cytochrome b6f Complex† William A. Cramer,* Huamin Zhang, Jiusheng Yan, Genji Kurisu,‡ and Janet L. Smith Department of Biological Sciences, Lilly Hall of Life Sciences, 915 West State Street, Purdue UniVersity, West Lafayette, Indiana 47907-2054 ReceiVed March 22, 2004; ReVised Manuscript ReceiVed April 7, 2004 ABSTRACT: Structures of the cytochrome b6f complex obtained from the thermophilic cyanobacterium Mastigocladus laminosus and the green alga Chlamydomonas reinhardtii, whose appearance in evolution is separated by 109 years, are almost identical. Two monomers with a molecular weight of 110 000, containing eight subunits and seven natural prosthetic groups, are separated by a large lipid-containing “quinone exchange cavity”. A unique heme, heme x, that is five-coordinated and high-spin, with no strong field ligand, occupies a position close to intramembrane heme bn. This position is filled by the n-side bound quinone, Qn, in the cytochrome bc1 complex of the mitochondrial respiratory chain. The structure and position of heme x suggest that it could function in ferredoxin-dependent cyclic electron transport as well as being an intermediate in a quinone cycle mechanism for electron and proton transfer. The significant differences between the cyanobacterial and algal structures are as follows. (i) On the n-side, a plastoquinone molecule is present in the quinone exchange cavity in the cyanobacterial complex, and a sulfolipid is bound in the algal complex at a position corresponding to a synthetic DOPC lipid molecule in the cyanobacterial complex. (ii) On the p-side, in both complexes a quinone analogue inhibitor, TDS, passes through a portal that separates the large cavity from a niche containing the Fe2S2 cluster.
    [Show full text]
  • Overexpression of the Rieske Fes Protein of the Cytochrome B6f
    bioRxiv preprint doi: https://doi.org/10.1101/574897; this version posted March 12, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Overexpression of the Rieske FeS protein of the Cytochrome b6f complex increases C4 photosynthesis Maria Ermakova1*, Patricia E. Lopez-Calcagno2, Christine A. Raines2, Robert T. Furbank1 and Susanne von Caemmerer1 1 Australian Research Council Centre of Excellence for Translational Photosynthesis, Division of Plant Science, Research School of Biology, The Australian National University, Acton, Australian Capital Territory 2601, Australia. 2 School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK. * Correspondence: [email protected] Abstract C4 plants contribute 20% to the global primary productivity despite representing only 4% of higher plant species. Their CO2 concentrating mechanism operating between mesophyll and bundle sheath cells increases CO2 partial pressure at the site of Rubisco and hence photosynthetic efficiency. Electron transport chains in both cell types supply ATP and NADPH for C4 photosynthesis. Since Cytochrome b6f is a key point of control of electron transport in C3 plants, we constitutively overexpressed the Rieske FeS subunit in Setaria viridis to study the effects on C4 photosynthesis. Rieske FeS overexpression resulted in a higher content of Cytochrome b6f in both mesophyll and bundle sheath cells without marked changes in abundances of other photosynthetic complexes and Rubisco. Plants with higher Cytochrome b6f abundance showed better light conversion efficiency in both Photosystems and could generate higher proton-motive force across the thylakoid membrane.
    [Show full text]