DOCSLIB.ORG

Proteorhodopsin Photosystem Gene Expression Enables Photophosphorylation in a Heterologous Host

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Proteorhodopsin Photosystem Gene Expression Enables Photophosphorylation in a Heterologous Host Proteorhodopsin photosystem gene expression enables photophosphorylation in a heterologous host A. Martinez*, A. S. Bradley†, J. R. Waldbauer‡, R. E. Summons†, and E. F. DeLong*§ *Department of Civil and Environmental Engineering, Division of Biological Engineering, and †Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139; and ‡Joint Program in Chemical Oceanography, Woods Hole Oceanographic Institution and Massachusetts Institute of Technology, Cambridge, MA 02139 Edited by W. Ford Doolittle, Dalhousie University, Halifax, NS, Canada, and approved February 9, 2007 (received for review December 22, 2006) Proteorhodopsins (PRs) are retinal-containing proteins that cata- To further characterize PR photosystem structure and func- lyze light-activated proton efflux across the cell membrane. These tion, we directly screened large-insert DNA libraries derived photoproteins are known to be globally distributed in the ocean’s from marine picoplankton for visibly detectable PR-expressing photic zone, and they are found in a diverse array of Bacteria and phenotypes. In this report, we describe completely intact PR- Archaea. Recently, light-enhanced growth rates and yields have based photosystems that can be functionally expressed in E. coli, been reported in at least one PR-containing marine bacterium, but without addition of exogenous photopigment (e.g., retinal or its the physiological basis of light-activated growth stimulation has precursors). Analyses of insertional mutants verified the func- not yet been determined. To describe more fully PR photosystem tional annotation of each gene product in the photosystem genetics and biochemistry, we functionally surveyed a marine biosynthetic pathway. We also show that light-activated, PR- picoplankton large-insert genomic library for recombinant clones catalyzed proton translocation, by the chemiosmotic potential it expressing PR photosystems in vivo. Our screening approach ex- generates, activates photophosphorylation in E. coli. ploited transient increases in vector copy number that significantly Results enhanced the sensitivity of phenotypic detection. Two genetically distinct recombinants, initially identified by their orange pigmen- Screening a Fosmid Library for in Vivo PR Photosystem Expression. tation, expressed a small cluster of genes encoding a complete When E. coli expresses a PR apoprotein from an inducible PR-based photosystem. Genetic and biochemical analyses of trans- promoter on a high-copy number plasmid, the cells acquire a red or orange pigmentation in the presence of exogenous all-trans poson mutants verified the function of gene products in the retinal (1, 12). Retinal addition is required because E. coli lacks photopigment and opsin biosynthetic pathways. Heterologous the ability to biosynthesize retinal or its precursor, ␤-carotene. expression of six genes, five encoding photopigment biosynthetic Based on these observations, we screened for PR-containing proteins and one encoding a PR, generated a fully functional PR clones on retinal-containing LB agar plating medium, which we photosystem that enabled photophosphorylation in recombinant expected would display an orange to red phenotype under these Escherichia coli cells exposed to light. Our results demonstrate that conditions. To enhance assay sensitivity, we used the copy- a single genetic event can result in the acquisition of phototrophic control system present in our fosmid vector that allowed a capabilities in an otherwise chemoorganotrophic microorganism, controlled transition from one copy per cell to multiple (up to and they explain in part the ubiquity of PR photosystems among 100) vector copies upon addition of the inducer L-arabinose (13). diverse microbial taxa. A fosmid library prepared from ocean surface water pico- plankton containing 12,280 clones (Ϸ440 Mb of cloned DNA) photoheterotrophy ͉ rhodopsin ͉ lateral gene transfer ͉ marine ͉ (14) was screened by using the above approach. Three orange metagenomics colonies were identified as potential PR-expressing clones on the LB-retinal-L-arabinose agar plates. All three showed no pigmen- roteorhodopsins (PRs) are retinal-binding membrane pro- tation in the absence of the high-copy number inducer. Unex- Pteins belonging to the rhodopsin family. Prokaryotic mem- pectedly, these clones also displayed an orange phenotype in the bers of this family include photosensors (sensory rhodopsins), absence of L-retinal when induced to high copy number. The transmembrane proton pumps (bacteriorhodopsins, xanthoro- sequence of one clone, HF10࿝19P19, revealed the presence of a hodopsin, and PRs), and transmembrane chloride pumps (halor- PR gene near the fosmid vector junction (see below). Because hodopsins). Originally discovered in Archaea, rhodopsins were the clones exhibited orange pigmentation in the absence of later identified in Gammaproteobacteria of the SAR86 group exogenous retinal, we expected that they must also be expressing ࿝ during a cultivation-independent genomic survey. Dubbed pro- retinal biosynthetic genes. Two clones, HF10 25F10 and teorhodopsin, this photoprotein functions as a light-activated proton pump when expressed in Escherichia coli in the presence Author contributions: A.M. and E.F.D. designed research; A.M., A.S.B., and J.R.W. per- of exogenously added retinal (1). Since then, numerous molec- formed research; A.M., A.S.B., J.R.W., R.E.S., and E.F.D. analyzed data; and A.M. and E.F.D. ular surveys have demonstrated that PR genes are ubiquitous in wrote the paper. bacteria inhabiting the ocean’s photic zone (2–9). An estimated The authors declare no conflict of interest. 13% of bacteria in marine picoplankton populations, as well as This article is a PNAS Direct Submission. a significant fraction of planktonic Euryarchaeota, contain a PR Abbreviations: CCCP, carbonylcyanide m-chlorophenylhydrazone; DCCD, N,NЈ-dicyclo- gene (4, 8). In a number of marine bacteria, retinal biosynthetic hexylcarbodiimide; FPP, farnesyl diphosphate; GGPP, geranylgeranyl pyrophosphate; IPP, genes and PR are genetically linked, and their lateral transfer isopentenyl diphosphate; PR, proteorhodopsin. and retention appear to be relatively common events, indicating Data deposition: The sequences reported in this paper have been deposited in the GenBank database [accession nos. EF100190 (HF10࿝19P19) and EF100191 (HF10࿝25F10)]. that the photosystem confers a significant fitness advantage (3, §To whom correspondence should be addressed at: Department of Civil and Environmental 4, 7, 10, 11). A recent report of light-stimulated growth in a Engineering, 48-427, Massachusetts Institute of Technology, 15 Vassar Street, Cambridge, PR-containing marine flavobacterium supports this hypothesis MA 02139. E-mail: [email protected]. (11). Despite all of these observations however, the various This article contains supporting information online at www.pnas.org/cgi/content/full/ specific functions and physiological roles of diverse marine 0611470104/DC1. microbial PRs remain to be fully described. © 2007 by The National Academy of Sciences of the USA 5590–5595 ͉ PNAS ͉ March 27, 2007 ͉ vol. 104 ͉ no. 13 www.pnas.org͞cgi͞doi͞10.1073͞pnas.0611470104 Downloaded by guest on September 29, 2021 A idi blh crtY crtB crtI crtE PR HF10_19P19 HF10_25F10 B HF10_19P19 idi blh crtY crtB crtI crtE PR C D IPP δ-isomerase (idi) IPP CH 2 O P P CH O P P DMAPP 2 Lycopene FPP synthase IPP CrtY - IPP nm λ=473nm 200 250 300 350 400 450 500 550 600 650 700 750 800 (ispA) λ (nm) Lycopene CH O P P - 2 FPP polyisoprenoids CrtY ubiquinones HF10_19P19 GGPP synthase IPP CrtI - Blh - crtE 25.00 30.00 35.00 40.00 45.00 50.00 Rt (min) CH 2 O P P GGPP Phytoene synthase GGPP crtB β-carotene Blh- n 200 250 300 350 400 450 500 550 600 650 700 750 800 Phytoene λ =454nm λ (nm) β-carotene Blh- Phytoene dehydrogenase HF10_19P19 crtI CrtY- CrtI- 20.00 25.00 30.00 35.00 40.00 45.00 Lycopene Rt (min) 1 9 .2 MICROBIOLOGY Lycopene cyclase crtY Retinal β-Carotene HF10_19P19 n λ=386nm 200 250 300 350 400 450 500 550 600 650 700 750 800 λ (nm) O Retinal 2 15,15’-β-carotene dioxygenase HF10_19P19 blh CrtY- CrtI- Blh- COH Retinal 10.0 0000 115.005 00 220.00 000 2525.0000 3030.00 00 3535.00 tR ( m )ni Fig. 1. Genetic and phenotypic analysis of PR photosystem transposon mutants. (A) Schematic representation of the PR gene clusters identified in this work. Predicted transcription terminators in the clusters are indicated. (B) Color phenotype of intact cells of transposon-insertion mutants grown in liquid cultures with arabinose. (C) Retinal biosynthesis pathway. Names of genes encoding pathway enzymes are indicated. The genes that are present in E. coli are in parentheses. (D) HPLC profiles of wild-type and transposon mutant extracts. Detection wavelengths are indicated. Absorption spectrum of relevant peaks, including standards used for identification, are shown on the top for each panel. HF10࿝19P19, were analyzed further for PR photosystem gene PR-containing BAC clones from Alphaproteobacteria from the expression and function. Mediterranean and Red Seas (8). This similarity was evident across the entire cloned insert, although some large-scale rear- Genomic Analyses of Candidate PR Photosystem-Expressing Clones. rangements were apparent. The HF10࿝19P19 PR-inferred pro- The full DNA sequence of the two putative PR photosystem- tein sequence was most similar to a homologue from another containing fosmids was obtained by sequencing a collection of environmental BAC, MedeBAC66A03
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]
  • Photosynthetic Phosphorylation Above and Below 00C by David 0
    VOL. 48, 1962 BIOCHEMISTRY: HALL AND ARNON 833 10 De Robertis, E., J. Biophy8. Biochem. Cytol., 2, 319 (1956). 11 Eakin, R. M., and J. A. Westfall, ibid., 8, 483 (1960). 12 Eakin, R. M., these PROCEEDINGS, 47, 1084 (1961). 13 Wolken, J. J., in The Structure of the Eye, ed. G. K. Smelser (New York: Academic Press, 1961). 14 Wald, G., ibid. 16 Eakin, R. M., and J. A. Westfall, Embryologia, 6, 84 (1961). 16 Sj6strand, F. S., in The Structure of the Eye, ed. G. K. Smelser (New York: Academic Press, 1961). 17 Miller, W. H., in The Cell, ed. J. Brachet and A. E. Mirsky (New York: Academic Press, 1960), part IV. 18 Miller, W. H., J. Biophys. Biochem. Cytol., 4, 227 (1958). 19 Hesse, R., Z. wiss. Zool., 61, 393 (1896). 20 Bradke, D. L., personal communication. 21 Wolken, J. J., Ann. N. Y. Acad. Sci., 74, 164 (1958). 22 Rohlich, P., and L. J. Torok, Z. wiss. Zool., 54, 362 (1961). 28 Eakin, R. M., and J. A. Westfall, J. Ultrastr. Res. (in press). 24 Franz, V., Jena. Z. Naturwiss., 59, 401 (1923). PHOTOSYNTHETIC PHOSPHORYLATION ABOVE AND BELOW 00C BY DAVID 0. HALL* AND DANIEL I. ARNONt DEPARTMENT OF CELL PHYSIOLOGY, UNIVERSITY OF CALIFORNIA, BERKELEY Read before the Academy, April 25, 1962 CO2 assimilation in photosynthesis consists of a series of dark enzymatic reactions that are driven solely by adenosine triphosphate and reduced pyridine nucleotide. 1-4 The same reactions are now known to operate in nonphotosynthetic cells.5-"3 It follows, therefore, that the distinction between carbon assimilation in photosyn- thetic and nonphotosynthetic cells lies in the manner in which ATP14 and PNH214 are formed.
    [Show full text]
  • Bacterial Photophosphorylation: Regulation by Redox Balance* by Subir K
    VOL. 49, 1963 BIOCHEMISTRY: BOSE AND GEST 337 12 Hanson, L. A., and I. Berggird, Clin. Chim. Acta, 7, 828 (1962). 13 Stevenson, G. T., J. Clin. Invest., 41, 1190 (1962). 14 Burtin, P., L. Hartmann, R. Fauvert, and P. Grabar, Rev. franc. etudes clin. et biol., 1, 17 (1956). 15 Korngold, L., and R. Lipari, Cancer, 9, 262 (1956). 16Lowry, 0. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem., 193, 265 (1951). 17 Muller-Eberhard, H. J., Scand. J. Clin. and Lab. Invest., 12, 33 (1960). 18 Bergg&rd, I., Arkiv Kemi, 18, 291 (1962). 19 BerggArd, I., Arkiv Kemi, 18, 315 (1962). 20 Flodin, P., Dextran Gels and Their Application in Gel Filtration (Uppsala: Pharmacia, 1962). 21 Dische, Z., and L. B. Shettles, J. Biol. Chem., 175, 595 (1948). 22 Kunkel, H. G., and R. Trautman, in Electrophoresis, ed. M. Bier (New York: Academic Press, 1959), p. 225. 23Fleischman, J. B., R. H. Pain, and R. R. Porter, Arch. Biochem. Biophys., Suppl. 1, 174 (1962). 24 Porter, R. R., Biochem. J., 73, 119 (1959). 25 Edelman, G. M., J. F. Heremans, M.-Th. Heremans, and H. G. Kunkel, J. Exptl. Med., 112, 203 (1960). 26 Scheidegger, J. J., Intern. Arch. Allergy Appl. Immunol., 7, 103 (1955). 27 Yphantis, D. A., American Chemical Society, 140th meeting, Chicago, Abstracts of Papers, 1961, p. ic. 28 Gally, J. A. and G. M. Edelman, Biochim. Biophys. Acta, 60, 499 (1962). 29 Webb, T., B. Rose, and A. H. Sehon, Can. J. Biochem. Physiol., 36, 1159 (1958).
    [Show full text]
  • Photosynthesis
    ENVIRONMENTAL PLANT PHYSIOLOGY SESSION 3 Photosynthesis An understanding of the biochemical processes of photosynthesis is needed to allow us to understand how plants respond to changing environmental conditions. This session looks at the details of the physiology and considers how plants can adapt these processes. If you studied the foundation degree with Myerscough previously you will recognise that much of these session notes are a very similar to those provided for the Plant Biology Module. The difference is not in the content but in the level of understanding required! Page Introduction to Photosynthesis 2 First catch your light! 3 The Light Dependent Reaction 7 The Light Independent Reaction 11 Photosynthesis and the Environment 12 Alternative Carbon Fixation Strategies 16 Further Reading 19 LEARNING OUTCOMES You need to be able to describe the biochemical basis of photosynthesis including: • Describing the role of chloroplasts and chlorophyll • Describing the steps of the light reaction and stating its products • Describing the Calvin cycle or light independent reaction and stating its products • Describing the role and position of the electron transport chain • Identify the effects of environmental factors on the rate of photosynthesis and explain how these relate to your field of study • Describe adaptations used by plants to continue photosynthesis in conditions of environmental stress such as hot arid conditions or shade conditions 1 Introduction to Photosynthesis The sun is the main source of energy to all living things. Light energy from the sun is converted to the chemical energy of organic molecules by green plants by a complicated pathway of reactions called photosynthesis.
    [Show full text]
  • Quantum Efficiency of Photosynthetic Energy Conversion (Photosynthesis/Photophosphorylation/Ferredoxin) RICHARD K
    Proc. Natl. Acad. Sd. USA Vol. 74, No. 8, pp. 3377-81, August 1977 Biophysics Quantum efficiency of photosynthetic energy conversion (photosynthesis/photophosphorylation/ferredoxin) RICHARD K. CHAIN AND DANIEL I. ARNON Department of Cell Physiology, University of California, Berkeley, Berkeley, California 94720 Contributed by Daniel I. Arnon, June 7,1977 ABSTRACT The quantum efficiency of photosynthetic with cyclic and noncyclic photophosphorylation and a "dark," energy conversion was investigated in isolated spinach chlo- enzymatic phase concerned with the assimilation of CO2 (8). roplasts by measurements of the quantum requirements of ATP has established that the formation by cyclic and noncyclic photophosphorylation cata- Fractionation of chloroplasts (9) light lyzed by ferredoxin. ATP formation had a requirement of about phase is localized in the membrane fraction (grana) that is 2 quanta per 1 ATP at 715 nm (corresponding to a requirement separable from the soluble stroma fraction which contains the of 1 quantum per electron) and a requirement of 4 quanta per enzymes of CO2 assimilation (10). Thus, in isolated and frac- ATP (corresponding to a requirement of 2 quanta per electron) tionated chloroplasts, investigations of photosynthetic quantum at 554 nm. When cyclic and noncyclic photophosphorylation efficiency can be focused solely on cyclic and noncyclic pho-. were operating concurrently at 554 nm, a total of about 12 account the conversion of quanta was required to generate the two NADPH and three ATP tophosphorylation, which jointly for needed for the assimilation of one CO2 to the level of glu- photon energy into chemical energy without the subsequent cose. or concurrent reactions of biosynthesis and respiration that cannot be avoided in whole cells.
    [Show full text]
  • Consequences of the Structure of the Cytochrome B6 F Complex for Its Charge Transfer Pathways ⁎ William A
    Biochimica et Biophysica Acta 1757 (2006) 339–345 http://www.elsevier.com/locate/bba Review Consequences of the structure of the cytochrome b6 f complex for its charge transfer pathways ⁎ William A. Cramer , Huamin Zhang Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA Received 17 January 2006; received in revised form 30 March 2006; accepted 24 April 2006 Available online 4 May 2006 Abstract At least two features of the crystal structures of the cytochrome b6 f complex from the thermophilic cyanobacterium, Mastigocladus laminosus and a green alga, Chlamydomonas reinhardtii, have implications for the pathways and mechanism of charge (electron/proton) transfer in the complex: (i) The narrow 11×12 Å portal between the p-side of the quinone exchange cavity and p-side plastoquinone/quinol binding niche, through which all Q/QH2 must pass, is smaller in the b6 f than in the bc1 complex because of its partial occlusion by the phytyl chain of the one bound chlorophyll a molecule in the b6 f complex. Thus, the pathway for trans-membrane passage of the lipophilic quinone is even more labyrinthine in the b6 f than in the bc1 complex. (ii) A unique covalently bound heme, heme cn, in close proximity to the n-side b heme, is present in the b6 f complex. The b6 f structure implies that a Q cycle mechanism must be modified to include heme cn as an intermediate between heme bn and plastoquinone bound at a different site than in the bc1 complex. In addition, it is likely that the heme bn–cn couple participates in photosytem + I-linked cyclic electron transport that requires ferredoxin and the ferredoxin: NADP reductase.
    [Show full text]
  • Chapter 19 Photophosphorylation
    Chapter 19 Part 3 Photophosphorylation Learning Goals: To Know 1. How energy of sunlight creates charge separation in the photosynthetic reaction complex and exciton transfer. 2. How electron transport is accompanied by the directional transport of protons across the membrane against their concentration gradient 3. Similarities and differences between plant-algal photosystems and bacterial photosystems. 4. How the electrochemical proton gradient drives synthesis of ATP by coupling the flow of protons via ATP synthase to conformational changes that favor formation of ATP in the active site 5. Roles of rhodopsins. Primary Production – Solar Energy Conversion Chloroplasts How do Photosynthetic Bacteria Fit in Here? Hill Reaction (driven by light) in Photophosphorylation 2 H2O + 2 A 2 AH2 + O2 “A” in Biological Systems = NADP+ so the Hill Reaction is: + + 2 H2O + 2 NADP 2 NADPH + 2H + O2 What Robert Hill in 1937 Actually Measured Was: The reduction of DCIP: going from blue to colorless. Electromagnetic Spectrum What is an Einstein? Light Energy Planck-Einstein Equation: E = h ν E = energy of a photon h = Planck’s Constant = 6.6 x 10-34 J.s v = vibration frequency ( of the wavelength of light; vibrational frequency increases with a decrease in wavelength ) In the text, E = hc/λ c/λ = v so red light, λ = 700 nm, c = 3x108m/s So that one red photon E = 2.83 x 10-19 J For an Einstein (a mole of photons) E = 168 kJ/einstein Chlorophyll a What is with the PINK ??? Phycobilins Carotenoids Photopigment Absorption Spectrum Chlorophyll Types Noon, Nov 18th: Surface Sun Light Spectra OE Pond Where is the Visible and Infra-red light ? Which one gets to the bottom? Noon, Nov 18th: Bottom The y-axis is in units of (einsteins/s)/m2 at each wavelength.
    [Show full text]
  • Effects of Low Concentrations of Ammonia and Methylamine
    Photophosphorylation by Chloroplasts: Effects of Low Concentrations of Ammonia and Methylamine Christoph Giersch Botanisches Institut der Universität Düsseldorf, Universitätsstr. 1, D-4000 Düsseldorf, Bundesrepublik Deutschland Z. Naturforsch. 37 c, 242-250 (1982); received December 23, 1981 Photophosphorylation, Uncoupling, Amines, Proton Motive Force, Chloroplasts, Chemiosmotic Theory Intact chloroplasts exposed to hypotonic assay conditions are capable of photophosphorylating exogenous ADP. The rate of phosphorylation by these unbroken plastids is increased by 10—50% upon the addition of low concentrations (< mM) of N H 3 or CH3NH 2. Stimulation of phosphory­ lation is abolished by washing chloroplasts with MgCl2. Evidence is presented that washing re­ moves a factor responsible for amine-induced increase of A TP production and that this factor is associated with the thylakoid membrane. Addition of CH3NH 2 increased the proton permeability of the thylakoid membrane of unbroken and washed chloroplasts during the light/dark transition. Hence, differences of the membrane permeability for protons between the two preparations seem not to be responsible for an increase of ATP production upon the addition of amines. Stimulation of photophosphorylation by methylamine is observed even at light itensities which do not saturate the proton motive force, which in turn is reduced upon the addition of the uncoupler. Apparently, phosphorylation can be stimulated, although the limiting driving force is diminished. It is con­ cluded that phosphorylation by unbroken chloroplasts under low light illumination is limited kinetically, not energetically. Consequences of these findings for observation made with intact chloroplasts are discussed. Introduction creased pmf in the presence of low amine * concen­ trations although the rate of steady-state light-de­ The chemiosmotic concept holds the trans­ pendent ATP production is increased [4].
    [Show full text]
  • BOOK REVIEWS Genes, Organisms, Populations: Controversies Over the Units of Selection Edited by Robert N
    BOOK REVIEWS Genes, organisms, populations: Controversies over the units of selection edited by Robert N. Brandon and Richard M. Burian. The MIT Press, Cambridge, Massachusetts, USA, 1984, -pp. xiv + 329, $ 34.44. He is a collection of papers on natural selection published over the'past 25 years. The unit (or units) of selection is the subject of discussion. Charles Darwin felt that the individual was the target of selection, not races, groups or populations. Alfred Wallace, on the other hand, thought that selection acted on groups in addition to the individual. Against this historical background of the two originators of the idea of natural selection, the editors have put together current views of selection, the levels as well as the units on which selection a&. The papers are grouped under three heads: Historical readings; Levels and units of selection; Models of selection. Each part has an introduction, contributed by the editors, who as students of philosophy appear to have found some sudden and unexplained interest in problems of evolution. Several of the papers included in the volume were written long before the question of natural selection hotted up some five years ago and so are of limited interest. Nevertheless, they are of considerable influence in determining the level at which selection is believed to operate. The main thrust of selection at levels higher than the individual level is offered by Altruism, which Darwin was clearly unaware of and which has only recently come to the fore. Seemingly contradictory, the different levels harmonize at a certain order; it seems to be the endeavour of the authors to find this conformation.
    [Show full text]
  • Do We Have a Thermotrophic Feature? James Weifu Lee
    www.nature.com/scientificreports OPEN Mitochondrial energetics with transmembrane electrostatically localized protons: do we have a thermotrophic feature? James Weifu Lee Transmembrane electrostatically localized protons (TELP) theory has been recently recognized as an important addition over the classic Mitchell’s chemiosmosis; thus, the proton motive force (pmf) is largely contributed from TELP near the membrane. As an extension to this theory, a novel phenomenon of mitochondrial thermotrophic function is now characterized by biophysical analyses of pmf in relation to the TELP concentrations at the liquid-membrane interface. This leads to the conclusion that the oxidative phosphorylation also utilizes environmental heat energy associated with the thermal kinetic energy (kBT) of TELP in mitochondria. The local pmf is now calculated to be in a range from 300 to 340 mV while the classic pmf (which underestimates the total pmf) is in a range from 60 to 210 mV in relation to a range of membrane potentials from 50 to 200 mV. Depending on TELP concentrations in mitochondria, this thermotrophic function raises pmf signifcantly by a factor of 2.6 to sixfold over the classic pmf. Therefore, mitochondria are capable of efectively utilizing the environmental heat energy with TELP for the synthesis of ATP, i.e., it can lock heat energy into the chemical form of energy for cellular functions. In the past, there was a common belief that the living organisms on Earth could only utilize light energy and/ or chemical energy, but not the environmental heat energy. Consequently, the life on Earth has been classifed as two types based on their sources of energy: phototrophs and chemotrophs.
    [Show full text]
  • BBA - Bioenergetics 1860 (2019) 433–438
    BBA - Bioenergetics 1860 (2019) 433–438 Contents lists available at ScienceDirect BBA - Bioenergetics journal homepage: www.elsevier.com/locate/bbabio Review The mechanism of cyclic electron flow T ⁎ W.J. Nawrockia,b, , B. Bailleula, D. Picotc, P. Cardolb, F. Rappaporta,1, F.-A. Wollmana, P. Joliota a Institut de Biologie Physico-Chimique, UMR 7141 CNRS-UPMC, 13 rue P. et M. Curie, 75005 Paris, France b Laboratoire de Génétique et Physiologie des Microalgues, Institut de Botanique, Université de Liège, 4, Chemin de la Vallée, B-4000 Liège, Belgium c Institut de Biologie Physico-Chimique, UMR 7099 CNRS-UPMC, 13 rue P. et M. Curie, 75005 Paris, France ARTICLE INFO ABSTRACT Keywords: Apart from the canonical light-driven linear electron flow (LEF) from water to CO2, numerous regulatory and Photosynthesis alternative electron transfer pathways exist in chloroplasts. One of them is the cyclic electron flow around Biophysics Photosystem I (CEF), contributing to photoprotection of both Photosystem I and II (PSI, PSII) and supplying extra Plastoquinone ATP to fix atmospheric carbon. Nonetheless, CEF remains an enigma in the field of functional photosynthesis as Cytochrome b f 6 we lack understanding of its pathway. Here, we address the discrepancies between functional and genetic/ Photosystem I biochemical data in the literature and formulate novel hypotheses about the pathway and regulation of CEF Cyclic electron flow based on recent structural and kinetic information. 1. Linear and cyclic electron flow kinetic and methodological standpoint in the light of our report that PGRL1 is not directly transferring electrons from Fd to PQ during CEF Photosynthesis consists of a photoinduced linear electron flow [1].
    [Show full text]
  • Chemiosmosis - the Mechanism of ATP Synthesis in Chloroplasts
    Chemiosmosis - The Mechanism of ATP Synthesis in Chloroplasts The thylakoid membrane is composed of a phospholipid bilayer (color phospholipids "B" light blue) and photosystem I and photosystem II. Although they both work simultaneously, it is best to look at them one at a time, starting with photosystem II. The first and most important event in either system is the capturing of light energy (color "E" orange) by the pigments associated with each photosystem. Color the pigments of Photosystem II (P2) dark green and the pigments of Photosystem I (P1) light green. Pigment 680 (color dark green) is associated with Photosystem II, and Pigment 700 (color light green) is associated with Photosystem I. When a photon of light strikes the reaction center of Photosystem II, it excites an electron. Two water molecules bind to an enzyme that splits water into hydrogen ions (protons) and releases an oxygen atom. Color the protons (H+) yellow and the oxygen atoms (O2) red. This process is called PHOTOLYSIS and is illustrated by the arrows labeled "L", which you should color pink. Two electrons are released in this process, and these electrons can be traced through photosystem II and photosystem I. Color the electrons (e) grey. Two oxygen atoms will join together to create an oxygen molecule which is released from the plant as a byproduct of the entire reaction. The primary electron acceptor for the light-energized electrons leaving photosystem II is plastoquinone (color PQ purple). The reduced plastoquinone passes the excited electrons to a proton pump embedded in the membrane called the b6-f complex (color dark blue).
    [Show full text]