Abstract
Halophilic archaea (haloarchaea) inhabit hypersaline environments, tolerating extreme salinity, low oxygen and nutrient availability, and in some cases, high pH (soda lakes) and irradiation (saltern ponds). Membrane-associated proteins of haloarchaea, such as surface layer (S-layer) proteins, transporters, retinal proteins, and internal organellar membrane proteins including intracellular gas vesicle proteins and those associated with polyhydroxyalkanoate (PHA) granules, contribute greatly to their environmental adaptations. This review focuses on these haloarchaeal cellular and organellar membrane-associated proteins, and provides insight into their physiological significance and biotechnological potential.
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DasSarma P, Klebahn G, Klebahn H. Translation of Henrich Klebahn’s’ Damaging agents of the klippfish-a contribution to the knowledge of the salt-loving organisms’. Saline Systems, 2010, 6:7
Woese C R, Magrum L J, Fox G E. Archaebacteria. J Mol Evol, 1978, 11:245–251
Soppa J. From genomes to function: haloarchaea as model organisms. Microbiol-Sgm, 2006, 152:585–590
Messner P, Sleytr U B. Crystalline bacterial cell-surface layers. Adv Microb Physiol, 1992, 33:213–275
Oren A. Bioenergetic aspects of halophilism. Microbiol Mol Biol Rev, 1999, 63:334–348
Albers S V, Van de Vossenberg J L, Driessen A J, et al. Bioenergetics and solute uptake under extreme conditions. Extremophiles, 2001, 5:285–294
Albers S V, Szabó Z, Driessen A J M. Protein secretion in the Archaea: multiple paths towards a unique cell surface. Nat Rev Microbiol, 2006, 4:537–547
Natale P, Brüser T, Driessen A J M. Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane Distinct translocases and mechanisms. BBA-Biomembranes, 2008, 1778: 1735–1756
Schäfer G, Engelhard M, Müller V. Bioenergetics of the archaea. Microbiol Mol Biol R, 1999, 63:570–620
Hampp N. Bacteriorhodopsin as a photochromic retinal protein for optical memories. Chem Rev, 2000, 100:1755–1776
Lanyi J K. Halorhodopsin: a light-driven chloride ion pump. Annu Rev Biophys Biophys Chem, 1986, 15:11–28
DasSarma S, DasSarma P. Halophiles. In: Encyclopedia of Life Sciences. Chichester: John Wiley & Sons, 2012
DasSarma S, Arora P. Genetic analysis of the gas vesicle gene cluster in haloarchaea. Fems Microbiol Lett, 1997, 153:1–10
Cai S, Cai L, Liu H, et al. Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei. Appl Environ Microbiol, 2012, 78:1946–1952
Lu Q H, Han J, Zhou L G, et al. Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthase in Haloferax mediterranei. J Bacteriol, 2008, 190:4173–4180
Han J, Lu Q, Zhou L, et al. Molecular characterization of the phaECHm, genes, required for biosynthesis of poly(3-hydroxybutyrate) in the extremely halophilic Archaeon Haloarcula marismortui. Appl Environ Microb, 2007, 73:6058–6065
Jendrossek D. Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes). J Bacteriol, 2009, 191:3195–3202
Baumeister W, Lembcke G. Structural features of archaebacterial cell envelopes. J Bioenerg Biomembr, 1992, 24:567–575
Baumeister W, Wildhaber I, Phipps B M. Principles of organization in eubacterial and archaebacterial surface-proteins. Can J Microbiol, 1989, 35:215–227
Houwink A L. Flagella, gas vacuoles and cell-wall structure in Halobacterium halobium: an electron microscope study. J Gen Microbiol, 1956, 15:146–150
Koga Y, Morii H. Recent advances in structural research on ether lipids from archaea including comparative and physiological aspects. Biosci Biotech Bioch, 2005, 69:2019–2034
Mescher M F, Hansen U, Strominger J L. Formation of lipid-linked sugar compounds in Halobacterium salinarium-presumed intermediates in glycoprotein synthesis. J Biol Chem, 1976, 251: 7289–7294
Wieland F, Lechner J, Bernhardt G, et al. Sulfation of a repetitive saccharide in halobacterial cell-wall glycoprotein occurrence of a sulfated lipid-linked precursor. Febs Lett, 1981, 132:319–323
Wakai H, Nakamura S, Kawasaki H, et al. Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1. Extremophiles, 1997, 1:29–35
Sumper M, Berg E, Mengele R, et al. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J Bacteriol, 1990, 172:7111–7118
Lechner J, Sumper M. The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem, 1987, 262:9724–9729
Fukuchi S, Yoshimune K, Wakayama M, et al. Unique amino acid composition of proteins in halophilic bacteria. J Mol Biol, 2003, 327:347–357
Madern D, Ebel C, Zaccai G. Halophilic adaptation of enzymes. Extremophiles, 2000, 4:91–98
Ng W V, Kennedy S P, Mahairas G G, et al. Genome sequence of Halobacterium species NRC-1. Proc Natl Acad Sci USA, 2000, 97:12176–12181
Sleytr U B, Thorne K J. Chemical characterization of the regularly arranged surface layers of Clostridium thermosaccharolyticum and Clostridium thermohydrosulfuricum. J Bacteriol, 1976, 126: 377–383
Yurist-Doutsch S, Chaban B, VanDyke D J, et al. Sweet to the extreme: protein glycosylation in Archaea. Mol Microbiol, 2008, 68:1079–1084
Abu-Qarn M, Yurist-Doutsch S, Giordano A, et al. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J Mol Biol, 2007, 374:1224–1236
Abu-Qarn M, Giordano A, Battaglia F, et al. Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein. J Bacteriol, 2008, 190:3140–3146
Plavner N, Eichler J. Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii. J Bacteriol, 2008, 190:8045–8052
Yurist-Doutsch S, Abu-Qarn M, Battaglia F, et al. aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol Microbiol, 2008, 69:1234–1245
Eichler J. Facing extremes: archaeal surface-layer (glyco)proteins. Microbiology, 2003, 149:3347–3351
Mengele R, Sumper M. Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles. J Biol Chem, 1992, 267:8182–8185
Le Dain A C, Saint N, Kloda A, et al. Mechanosensitive ion channels of the archaeon Haloferax volcanii. J Biol Chem, 1998, 273:12116–12119
Häse C C, Ledain A C, Martinac B. Purification and functional reconstitution of the recombinant large mechanosensitive ion-channel (Mscl) of Escherichia coli. J Biol Chem, 1995, 270:18329–18334
Higgins C F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol, 1992, 8:67–113
Albers S V, Koning S M, Konings W N, et al. Insights into ABC transport in archaea. J Bioenerg Biomembr, 2004, 36:5–15
Wanner C, Soppa J. Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii. Genetics, 1999, 152:1417–1428
Woodson J D, Reynolds A A, Escalante-Semerena J C. ABC transporter for corrinoids in Halobacterium sp strain NRC-1. J Bacteriol, 2005, 187:5901–5909
Lee S J, Böhm A, Krug M, et al. The ABC of binding-protein-dependent transport in archaea. Trends Microbiol, 2007, 15: 389–397
Bolhuis H, Palm P, Wende A, et al. The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity. BMC Genomics, 2006, 7:169
Barabote R D, Saier M H Jr. Comparative genomic analyses of the bacterial phosphotransferase system. Microbiol Mol Biol Rev, 2005, 69:608–634
Anderson I, Rodriguez J, Susanti D, et al. Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction. J Bacteriol, 2008, 190: 2957–2965
Bolhuis A. Protein transport in the halophilic archaeon Halobacterium sp NRC-1:a major role for the twin-arginine translocation pathway? Microbiol-Sgm, 2002, 148:3335–3346
Hutcheon G W, Bolhuis A. The archaeal twin-arginine translocation pathway. Biochem Soc T, 2003, 31:686–689
Gimenez M I, Dilks K, Pöhlschroder M. Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins. Mol Microbiol, 2007, 66:1597–1606
Berks B C, Palmer T, Sargent F. Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr Opin Microbiol, 2005, 8:174–181
Rose R W, Brüser T, Kissinger J C, et al. Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol Microbiol, 2002, 45:943–950
Widdick D A, Eijlander R T, van Dijl J M, et al. A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life. J Mol Biol, 2008, 375:595–603
Berks B C, Palmer T, Sargent F. The Tat protein translocation pathway and its role in microbial physiology. Adv Microb Physiol, 2003, 47:187–254
Dilks K, Giménez M I, Pöhlschroder M. Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. J Bacteriol, 2005, 187:8104–8113
Sargent F. The twin-arginine transport system: moving folded proteins across membranes. Biochem Soc Trans, 2007, 35:835–847
Thomas J R, Bolhuis A. The tatC gene cluster is essential for viability in halophilic archaea. FEMS Microbiol Lett, 2006, 256:44–49
Spudich J L, Yang C S, Jung K H, et al. Retinylidene proteins: structures and functions from archaea to humans. Annu Rev Cell Dev Biol, 2000, 16:365–392
Spudich J L. Variations on a molecular switch: transport and sensory signalling by archaeal rhodopsins. Mol Microbiol, 1998, 28: 1051–1058
Oesterhelt D, Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol, 1971, 233:149–152
Henderson R, Unwin P N T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature, 1975, 257:28–32
Subramaniam S, Hirai T, Henderson R. From structure to mechanism: electron crystallographic studies of bacteriorhodopsin. Philos T Roy Soc A, 2002, 360:859–874
Khorana H G. Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J Biol Chem, 1988, 263:7439–7442
Krebs M P, Hauss T, Heyn M P, et al. Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmid. Proc Natl Acad Sci USA, 1991, 88:859–863
Peck R F, Echavarri-Erasun C, Johnson E A, et al. brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum. J Biol Chem, 2001, 276:5739–5744
Oesterhelt D, Stoeckenius W. Functions of a new photoreceptor membrane. Proc Natl Acad Sci USA, 1973, 70:2853–2857
Stoeckenius W, Bogomolni R A. Bacteriorhodopsin and related pigments of halobacteria. Annu Rev Biochem, 1982, 51:587–616
Jin Y D, Friedman N, Sheves M, et al. Bacteriorhodopsin (bR) as an electronic conduction medium: Current transport through bR-containing monolayers. Proc Natl Acad Sci USA, 2006, 103:8601–8606
Lanyi J K. X-ray crystallography of bacteriorhodopsin and its photointermediates: Insights into the mechanism of proton transport. Biochemistry(Moscow), 2001, 66:1192–1196
Zhang F, Vierock J, Yizhar O, et al. The microbial opsin family of optogenetic tools. Cell, 2011, 147:1446–1457
Hirai T, Subramaniam S. Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses. PLoS ONE, 2009, 4:e5769
Lozier R H, Bogomolni R A, Stoeckenius W. Bacteriorhodopsin: a light-driven proton pump in Halobacterium halobium. Biophys J, 1975, 15:955–962
Krebs M P, Khorana H G. Mechanism of light-dependent proton translocation by bacteriorhodopsin. J Bacteriol, 1993, 175: 1555–1560
Dioumaev A K, Lanyi J K. Bacteriorhodopsin photocycle at cryogenic temperatures reveals distributed barriers of conformational substates. Proc Natl Acad Sci USA, 2007, 104:9621–9626
Schobert B, Lanyi J K. Halorhodopsin is a light-driven chloride pump. J Biol Chem, 1982, 257:306–313
Kolbe M, Besir H, Essen L O, et al. Structure of the light-driven chloride pump halorhodopsin at 1.8 angstrom resolution. Science, 2000, 288:1390–1396
Hegemann P, Oesterhelt D, Steiner M. The photocycle of the chloride pump halorhodopsin I: azidecatalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump. EMBO J, 1985, 4:2347–2350
Kunji E R S, von Gronau S, Oesterhelt D, et al. The three-dimensional structure of halorhodopsin to 5 angstrom by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure. Proc Natl Acad Sci USA, 2000, 97:4637–4642
Mukohata Y, Ihara K, Tamura T, et al. Halobacterial rhodopsins. J Biochem, 1999, 125:649–657
Bogomolni R A, Spudich J L. Identification of a 3rd-rhodopsin-like pigment in phototactic Halobacterium halobium. Proc Natl Acad Sci-Biol, 1982, 79:6250–6254
Hoff W D, Jung K H, Spudich J L. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu Rev Bioph Biom, 1997, 26:223–258
Lutz I, Sieg A, Wegener A A, et al. Primary reactions of sensory rhodopsins. Proc Natl Acad Sci USA, 2001, 98:962–967
Sasaki J, Spudich J L. Proton circulation during the photocycle of sensory rhodopsin II. Biophys J, 1999, 77:2145–2152
Birge R R. Photophysics and molecular electronic applications of the rhodopsins. Annu Rev Phys Chem, 1990, 41:683–733
Yan B, Nakanishi K, Spudich J L. Mechanism of activation of sensory rhodopsin I: evidence for a steric trigger. Proc Natl Acad Sci USA, 1991, 88:9412–9416
Bergo V B, Spudich E N, Rothschild K J, et al. Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer. J Biol Chem, 2005, 280:28365–28369
Shively J M, Cannon G C, Heinhorst S, et al. Bacterial and Archaeal Inclusions. In: Encyclopedia of Life Sciences. Chichester: John Wiley & Sons, 2011
Offner S, Hofacker A, Wanner G, et al. Eight of fourteen gvp genes are sufficient for formation of gas vesicles in halophilic archaea. J Bacteriol, 2000, 182:4328–4336
DasSarma S, Arora P, Lin F, et al. Wild-type gas vesicle formation requires at least ten genes in the gvp gene cluster of Halobacterium halobium plasmid pNRC100. J Bacteriol, 1994, 176:7646–7652
Sivertsen A C, Bayro M J, Belenky M, et al. Solid-state NMR characterization of gas vesicle structure. Biophys J, 2010, 99:1932–1939
Strunk T, Hamacher K, Hoffgaard F, et al. Structural model of the gas vesicle protein GvpA and analysis of GvpA mutants in vivo. Mol Microbiol, 2011, 81:56–68
Hayes P K, Buchholz B, Walsby A E. Gas vesicles are strengthened by the outer-surface protein, GvpC. Arch Microbiol, 1992, 157:229–234
Halladay J T, Jones J G, Lin F, et al. The rightward gas vesicle operon in Halobacterium plasmid pNRC100: identification of the gvpA and gvpC gene products by use of antibody probes and genetic analysis of the region downstream of gvpC. J Bacteriol, 1993, 175: 684–692
Englert C, Pfeifer F. Analysis of gas vesicle gene expression in Haloferax mediterranei reveals that GvpA and GvpC are both gas vesicle structural proteins. J Biol Chem, 1993, 268:9329–9336
Offner S, Wanner G, Pfeifer F. Functional studies of the gvpACNO operon of Halobacterium salinarium reveal that the GvpC protein shapes gas vesicles. J Bacteriol, 1996, 178:2071–2078
Walsby A E. Gas vesicles. Microbiol Rev, 1994, 58:94–144
Shukla H D, DasSarma S. Complexity of gas vesicle biogenesis in Halobacterium sp. strain NRC-1: identification of five new proteins. J Bacteriol, 2004, 186:3182–3186
Chu L J, Chen M C, Setter J, et al. New structural proteins of Halobacterium salinarum gas vesicle revealed by comparative proteomics analysis. J Proteome Res, 2011, 10:1170–1178
Hezayen F F, Gutiérrez M C, Steinbüchel A, et al. Halopiger aswanensis sp. nov., a polymer-producing and extremely halophilic archaeon isolated from hypersaline soil. Int J Syst Evol Microbiol, 2010, 60:633–637
Lillo J G, Rodriguez-Valera F. Effects of culture conditions on poly(beta-hydroxybutyric acid) production by Haloferax mediterranei. Appl Environ Microbiol, 1990, 56:2517–2521
Hezayen F F, Rehm B H A, Eberhardt R, et al. Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor. Appl Microbiol Biot, 2000, 54:319–325
Rehm B H. Polyester synthases: natural catalysts for plastics. Biochem J, 2003, 376:15–33
Pötter M, Madkour M H, Mayer F, et al. Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16. Microbiology, 2002, 148:2413–2426
Pötter M, Steinbüchel A. Poly(3-hydroxybutyrate) granule-associated proteins: impacts on poly(3-hydroxybutyrate) synthesis and degradation. Biomacromolecules, 2005, 6:552–560
York G M, Stubbe J, Sinskey A J. The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production. J Bacteriol, 2002, 184:59–66
DasSarma P, Coker J A, Huse V, et al. Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Cell Technology. Chichester: John Wiley & Sons, 2010. 1–43
Sleytr U B, Huber C, Ilk N, et al. S-layers as a tool kit for nanobiotechnological applications. FEMS Microbiol Lett, 2007, 267: 131–144
Sleytr U B, Egelseer E M, Ilk N, et al. S-Layers as a basic building block in a molecular construction kit. FEBS J, 2007, 274:323–334
Sleytr U B, Sára M. Bacterial and archaeal S-layer proteins: structure-function relationships and their biotechnological applications. Trends Biotechnol, 1997, 15:20–26
Schäffer C, Messner P. Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology. Glycobiology, 2004, 14:31R–42R
Schuster B, Sleytr U B. Composite S-layer lipid structures. J Struct Biol, 2009, 168:207–216
Birge R R, Gillespie N B, Izaguirre E W, et al. Biomolecular electronics: Protein-based associative processors and volumetric memories. J Phys Chem B, 1999, 103:10746–10766
Stuart J A, Marcy D L, Wise K J, et al. Volumetric optical memory based on bacteriorhodopsin. Synthetic Met, 2002, 127:3–15
Li Q, Stuart J A, Birge R R, et al. Photoelectric response of polarization sensitive bacteriorhodopsin films. Biosens Bioelectron, 2004, 19:869–874
Birge R R. Protein-based computers. Sci Am, 1995, 272:90–95
Bodo C. Sensory systems: Back into the light. Nat Rev Neurosci, 2010, 11, doi: 10.1038/nrn2893
Busskamp V, Duebel J, Balya D, et al. Genetic reactivation of cone photoreceptors restores visual responses in retinitis pigmentosa. Science, 2010, 329:413–417
Cepko C. Neuroscience. Seeing the light of day. Science, 2010, 329:403–404
Walsby A E, Hayes P K. Gas vesicle proteins. Biochem J, 1989, 264:313–322
Stuart E S, Morshed F, Sremac M, et al. Antigen presentation using novel particulate organelles from halophilic archaea. J Biotechnol, 2001, 88:119–128
Stuart E S, Morshed F, Sremac M, et al. Cassette-based presentation of SIV epitopes with recombinant gas vesicles from halophilic archaea. J Biotechnol, 2004, 114:225–237
Sremac M, Stuart E S. Recombinant gas vesicles from Halobacterium sp. displaying SIV peptides demonstrate biotechnology potential as a pathogen peptide delivery vehicle. BMC Biotechnol, 2008, 8:9
Chen G Q, Wu Q. The application of polyhydroxyalkanoates as tissue engineering materials. Biomaterials, 2005, 26:6565–6578
Misra S K, Valappil S P, Roy I, et al. Polyhydroxyalkanoate (PHA)/inorganic phase composites for tissue engineering applications. Biomacromolecules, 2006, 7:2249–2258
Sodian R, Sperling J S, Martin D P, et al. Fabrication of a trileaflet heart valve scaffold from a polyhydroxyalkanoate biopolyester for use in tissue engineering. Tissue Eng, 2000, 6:183–188
Williams S F, Martin D P, Horowitz D M, et al. PHA applications: Addressing the price performance issue I. Tissue engineering. Int J Biol Macromol, 1999, 25:111–121
Peters V, Rehm B H A. In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl Environ Microb, 2006, 72:1777–1783
Brockelbank J A, Peters V, Rehm B H A. Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification. Appl Environ Microb, 2006, 72:7394–7397
Grage K, Rehm B H A. In vivo production of scFv-Displaying biopolymer beads using a self-assembly-promoting fusion partner. Bioconjugate Chem, 2008, 19:254–262
Peters V, Rehm B H A. Protein engineering of streptavidin for in vivo assembly of streptavidin beads. J Biotechnol, 2008, 134: 266–274
Jahns A C, Haverkamp R G, Rehm B H A. Multifunctional inorganic-binding beads self-assembled inside engineered bacteria. Bioconjugate Chem, 2008, 19:2072–2080
Banki M R, Wood D W. Inteins and affinity resin substitutes for protein purification and scale up. Microb Cell Fact, 2005, 4:32
Anderson A J, Dawes E A. Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiol Rev, 1990, 54:450–472
Lee S J, Park J P, Park T J, et al. Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads. Anal Chem, 2005, 77:5755–5759
Banki M R, Gerngross T U, Wood D W. Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Sci, 2005, 14:1387–1395
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Cai, L., Zhao, D., Hou, J. et al. Cellular and organellar membrane-associated proteins in haloarchaea: Perspectives on the physiological significance and biotechnological applications. Sci. China Life Sci. 55, 404–414 (2012). https://doi.org/10.1007/s11427-012-4321-z
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DOI: https://doi.org/10.1007/s11427-012-4321-z