Serpins in rice: protein sequence analysis, phylogeny and gene expression during development
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  • 作者:Sheila E Francis (1)
    Renan A Ersoy (1)
    Joon-Woo Ahn (1) (4)
    Brian J Atwell (2)
    Thomas H Roberts (1) (3)
  • 关键词:Serpin ; Protease inhibitor ; Rice ; Oryza sativa ; Arabidopsis thaliana ; Expression
  • 刊名:BMC Genomics
  • 出版年:2012
  • 出版时间:December 2012
  • 年:2012
  • 卷:13
  • 期:1
  • 全文大小:1586KB
  • 参考文献:1. Rawlings ND: Peptidase inhibitors in the MEROPS database. / Biochimie 2010, 92:1463鈥?483. CrossRef
    2. Law RHP, Zhang QW, McGowan S, Buckle AM, Silverman GA, Wong W, Rosado CJ, Langendorf CG, Pike RN, Bird PI, / et al.: An overview of the serpin superfamily. / Genome Biol 2006, 7:216. CrossRef
    3. Silverman GA, Whisstock JC, Bottomley SP, Huntington JA, Kaiserman D, Luke CJ, Pak SC, Reichhart JM, Bird PI: Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems. / J Biol Chem 2010, 285:24299鈥?4305. CrossRef
    4. Rau JC, Beaulieu LM, Huntington JA, Church FC: Serpins in thrombosis, hemostasis and fibrinolysis. / J Thromb Haemost 2007,5(Suppl 1):102鈥?15. CrossRef
    5. Huber R, Carrell RW: Implications of the three-dimensional structure of alpha 1- antitrypsin for structure and function of serpins. / Biochemistry 1989, 28:8951鈥?966. CrossRef
    6. Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PGW, Irving JA, Lomas DA, Luke CJ, Moyer RW, / et al.: The serpins are an expanding superfamily of structurally similar but functionally diverse proteins - Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. / J Biol Chem 2001, 276:33293鈥?3296. CrossRef
    7. Lampl N, Budai-Hadrian O, Davydov O, Joss TV, Harrop SJ, Curmi PM, Roberts TH, Fluhr R: Arabidopsis AtSerpin1: crystal structure and in vivo interaction with its target protease responsive to desiccation-21 (RD21). / J Biol Chem 2010, 285:13550鈥?3560. CrossRef
    8. Whisstock JC, Silverman GA, Bird PI, Bottomley SP, Kaiserman D, Luke CJ, Pak SC, Reichhart JM, Huntington JA: Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions. / J Biol Chem 2010, 285:24307鈥?4312. CrossRef
    9. Carrell RW, Evans DL, Stein PE: Mobile reactive centre of serpins and the control of thrombosis. / Nature 1991, 353:576鈥?78. CrossRef
    10. Schechter I, Berger A: On the size of the active site in proteases. I. Papain. / Biochem Biophys Res Commun 1967, 27:157鈥?62. CrossRef
    11. Lawrence DA, Ginsburg D, Day DE, Berkenpas MB, Verhamme IM, Kvassman JO, Shore JD: Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. / J Biol Chem 1995, 270:25309鈥?5312. CrossRef
    12. Stratikos E, Gettins PG: Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 脜 and full insertion of the reactive center loop into beta-sheet A. / Proc Natl Acad Sci USA 1999, 96:4808鈥?813. CrossRef
    13. Huntington JA, Read RJ, Carrell RW: Structure of a serpin-protease complex shows inhibition by deformation. / Nature 2000, 407:923鈥?26. CrossRef
    14. Carrell RW, Owen MC: Plakalbumin, alpha 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. / Nature 1985, 317:730鈥?32. CrossRef
    15. Dementiev A, Dobo J, Gettins PG: Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase. / J Biol Chem 2006, 281:3452鈥?457. CrossRef
    16. Chaillan-Huntington CE, Gettins PGW, Huntington JA, Patston PA: The P6-P2 region of serpins is critical for proteinase inhibition and complex stability. / Biochemistry 1997, 36:9562鈥?570. CrossRef
    17. Plotnick MI, Schechter NM, Wang ZM, Liu X, Rubin H: Role of the P6-P3' region of the serpin reactive loop in the formation and breakdown of the inhibitory complex. / Biochemistry 1997, 36:14601鈥?4608. CrossRef
    18. Stein PE, Tewkesbury DA, Carrell RW: Ovalbumin and angiotensinogen lack serpin S鈥揜 conformational change. / Biochem J 1989, 262:103鈥?07.
    19. Klieber MA, Underhill C, Hammond GL, Muller YA: Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release. / J Biol Chem 2007, 282:29594鈥?9603. CrossRef
    20. Zhou A, Wei Z, Read RJ, Carrell RW: Structural mechanism for the carriage and release of thyroxine in the blood. / Proc Natl Acad Sci USA 2006, 103:13321鈥?3326. CrossRef
    21. Hejgaard J, Roberts TH: Plant Serpins. In / Molecular and Cellular Aspects of the Serpinopathies and Disorders in Serpin Activity. Edited by: Silverman GA, Lomas DA. New Jersey: World Scientific; 2007:279鈥?00. CrossRef
    22. Roberts TH, Hejgaard J: Serpins in plants and green algae. / Funct Integr Genomics 2008, 8:1鈥?7. CrossRef
    23. Fluhr R, Lampl N, Roberts TH: Serpin protease inhibitors in plant biology. / Physiol Plant
    24. Fetterer RH, Miska KB, Jenkins M, Barfield R, Lillehoj H: Identification and characterization of a serpin from Eimeria acervulina . / J Parasitol 2008, 1.
    25. Roberts TH, Hejgaard J, Saunders NFW, Cavicchioli R, Curmi PMG: Serpins in unicellular Eukarya, Archaea, and Bacteria : Sequence analysis and evolution. / J Mol Evol 2004, 59:437鈥?47. CrossRef
    26. Riahi Y, Siman-Tov R, Ankri S: Molecular cloning, expression and characterization of a serine proteinase inhibitor gene from Entamoeba histolytica . / Mol Biochem Parasitol 2004, 133:153鈥?62. CrossRef
    27. Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC: The 1.5 angstrom crystal structure of a prokaryote serpin: Controlling conformational change in a heated environment. / Structure 2003, 11:387鈥?97. CrossRef
    28. Irving JA, Steenbakkers PJM, Lesk AM, den Camp HJMO, Pike RN, Whisstock JC: Serpins in prokaryotes. / Mol Biol Evol 2002, 19:1881鈥?890. fordjournals.molbev.a004012">CrossRef
    29. Zhang Q, Law R, Buckle AM, Cabrita L, McGowan S, Irving JA, Faux NG, Lesk AM, Bottomley SP, Whisstock JC: Serpins in Prokaryotes. In / Molecular and Cellular Aspects of the Serpinopathies and Disorders in Serpin Activity. Edited by: Silverman GA, Lomas DA. New Jersey: World Scientific; 2007:131鈥?62. CrossRef
    30. Dahl SW, Rasmussen SK, Hejgaard J: Heterologous expression of three plant serpins with distinct inhibitory specificities. / J Biol Chem 1996, 271:25083鈥?5088. CrossRef
    31. Dahl SW, Rasmussen SK, Petersen LC, Hejgaard J: Inhibition of coagulation factors by recombinant barley serpin BSZx. / FEBS Lett 1996, 394:165鈥?68. CrossRef
    32. Hejgaard J, Hauge S: Serpins of oat ( Avena sativa ) grain with distinct reactive centres and inhibitory specificity. / Physiol Plant 2002, 116:155鈥?63. CrossRef
    33. Hejgaard J, Laing WA, Marttila S, Gleave AP, Roberts TH: Serpins in fruit and vegetative tissues of apple ( Malus domestica ): expression of four serpins with distinct reactive centres and characterisation of a major inhibitory seed form, MdZ1b. / Funct Plant Biol 2005, 32:517鈥?27. CrossRef
    34. Ostergaard H, Rasmussen SK, Roberts TH, Hejgaard J: Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins - Cloning and characterization of five major molecular forms. / J Biol Chem 2000, 275:33272鈥?3279. CrossRef
    35. Rasmussen SK, Dahl SW, Norgard A, Hejgaard J: A recombinant wheat serpin with inhibitory activity. / Plant Mol Biol 1996, 30:673鈥?77. CrossRef
    36. Yoo BC, Aoki K, Xiang Y, Campbell LR, Hull RJ, Xoconostle-Cazares B, Monzer J, Lee JY, Ullman DE, Lucas WJ: Characterization of Cucurbita maxima phloem serpin-1 (CmPS-1) - A developmentally regulated elastase inhibitor. / J Biol Chem 2000, 275:35122鈥?5128. CrossRef
    37. Vercammen D, Belenghi B, van de Cotte B, Beunens T, Gavigan JA, De Rycke R, Brackenier A, Inze D, Harris JL, Van Breusegem F: Serpin1 of Arabidopsis thaliana is a suicide inhibitor for Metacaspase 9. / J Mol Biol 2006, 364:625鈥?36. CrossRef
    38. Wang Z, Gu C, Colby T, Shindo T, Balamurugan R, Waldmann H, Kaiser M, van der Hoorn RA: Beta-lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana . / Nat Chem Biol 2008, 4:557鈥?63. CrossRef
    39. Ahn JW, Atwell BJ, Roberts TH: Serpin genes AtSRP2 and AtSRP3 are required for normal growth sensitivity to a DNA alkylating agent in Arabidopsis . / BMC Plant Biol 2009, 9:52. CrossRef
    40. Chenna R, Sugawara H, Koike T, Lopez R, Gibson TJ, Higgins DG, Thompson JD: Multiple sequence alignment with the Clustal series of programs. / Nucl Acids Res 2003, 31:3497鈥?500. CrossRef
    41. Zhou AW, Carrell RW, Huntington JA: The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop. / J Biol Chem 2001, 276:27541鈥?7547. CrossRef
    42. Swofford DL: / PAUP. Phylogenetic analysis using parsimony (and other methods). Version 4 edition. Sinauer and Associates, Sunderland, Massachusetts; 2002.
    43. Page RD: Visualizing phylogenetic trees using TreeView. / Curr Protoc Bioinform 2002. Chapter 6: Unit 6 2.
    44. Hejgaard J: Purification and properties of protein Z - a major albumin of barley endosperm. / Physiol Plant 1982, 54:174鈥?82. CrossRef
    45. Carrell R, Travis J: Alpha1-antitrypsin and the serpins: variation and countervariation. / Trends Biochem Sci 1985, 10:20鈥?4. CrossRef
    46. Yeu SY, Park BS, Sang WG, Choi YD, Kim MC, Song JT, Paek N-C, Koh H-J, Seo HS: The serine proteinase inhibitor OsSerpin is a potent tillering regulator in rice. / J Plant Biol 2007, 50:600鈥?04. CrossRef
    47. Lesk AM: / Introduction to Protein Architecture. Oxford: Oxford University Press; 2001.
    48. Irving JA, Pike RN, Lesk AM, Whisstock JC: Phylogeny of the serpin superfamily. Implications of amino acid conservation for structure and function. / Genome Res 2000, 10:1845鈥?864. CrossRef
    49. Giese H, Hejgaard J: Synthesis of salt-soluble proteins in barley. / Pulse-labeling study of grain filling in liquid-cultured detached spikes. Planta 1984, 161:172鈥?77.
    50. Brandt A, Svendsen I, Hejgaard J: A plant serpin gene. Structure, organization and expression of the gene encoding barley protein Z4. / Eur J Biochem 1990, 194:499鈥?05. CrossRef
    51. Koller A, Washburn MP, Lange BM, Andon NL, Deciu C, Haynes PA, Hays L, Schieltz D, Ulaszek R, Wei J, / et al.: Proteomic survey of metabolic pathways in rice. / Proc Natl Acad Sci USA 2002, 99:11969鈥?1974. CrossRef
    52. Roberts TH, Marttila S, Rasmussen SK, Hejgaard J: Differential gene expression for suicide-substrate serine proteinase inhibitors (serpins) in vegetative and grain tissues of barley. / J Exp Bot 2003, 54:2251鈥?263. CrossRef
    53. Chichkova NV, Shaw J, Galiullina RA, Drury GE, Tuzhikov AI, Kim SH, Kalkum M, Hong TB, Gorshkova EN, Torrance L, / et al.: Phytaspase, a relocalisable cell death promoting plant protease with caspase specificity. / EMBO J 2010, 29:1149鈥?161. CrossRef
    54. Hejgaard J: Inhibitory serpins from rye grain with glutamine as P-1 and P-2 residues in the reactive center. / FEBS Lett 2001, 488:149鈥?53. CrossRef
    55. Hejgaard J: Inhibitory plant serpins with a sequence of three glutamine residues in the reactive center. / Biol Chem 2005, 386:1319鈥?323. CrossRef
    56. Levashina EA, Langley E, Green C, Gubb D, Ashburner M, Hoffmann JA, Reichhart JM: Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila . / Science 1999, 285:1917鈥?919. CrossRef
    57. Gettins PGW: Serpin structure, mechanism, and function. / Chem Rev 2002, 102:4751鈥?803. CrossRef
    58. Bajguz A, Hayat S: Effects of brassinosteroids on the plant responses to environmental stresses. / Plant Physiol Biochem 2009, 47:1鈥?. CrossRef
    59. la Cour Petersen M, Hejgaard J, Thompson GA, Schulz A: Cucurbit phloem serpins are graft-transmissible and appear to be resistant to turnover in the sieve element-companion cell complex. / J Exp Bot 2005, 56:3111鈥?120. CrossRef
  • 作者单位:Sheila E Francis (1)
    Renan A Ersoy (1)
    Joon-Woo Ahn (1) (4)
    Brian J Atwell (2)
    Thomas H Roberts (1) (3)

    1. Department of Chemistry and Biomolecular Sciences, Macquarie University, North Ryde, NSW, 2109, Australia
    4. Green Bio Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 111 Gwahangno, Yuseong-gu, Daejeon, 305-806, Korea
    2. Department of Biological Sciences, Macquarie University, North Ryde, NSW, 2109, Australia
    3. Department of Plant and Food Sciences, Faculty of Agriculture and Environment, University of Sydney, Sydney, NSW, 2006, Australia
文摘
Background Most members of the serpin family of proteins are potent, irreversible inhibitors of specific serine or cysteine proteinases. Inhibitory serpins are distinguished from members of other families of proteinase inhibitors by their metastable structure and unique suicide-substrate mechanism. Animal serpins exert control over a remarkable diversity of physiological processes including blood coagulation, fibrinolysis, innate immunity and aspects of development. Relatively little is known about the complement of serpin genes in plant genomes and the biological functions of plant serpins. Results A structurally refined amino-acid sequence alignment of the 14 full-length serpins encoded in the genome of the japonica rice Oryza sativa cv. Nipponbare (a monocot) showed a diversity of reactive-centre sequences (which largely determine inhibitory specificity) and a low degree of identity with those of serpins in Arabidopsis (a eudicot). A new convenient and functionally informative nomenclature for plant serpins in which the reactive-centre sequence is incorporated into the serpin name was developed and applied to the rice serpins. A phylogenetic analysis of the rice serpins provided evidence for two main clades and a number of relatively recent gene duplications. Transcriptional analysis showed vastly different levels of basal expression among eight selected rice serpin genes in callus tissue, during seedling development, among vegetative tissues of mature plants and throughout seed development. The gene OsSRP-LRS (Os03g41419), encoding a putative orthologue of Arabidopsis AtSerpin1 (At1g47710), was expressed ubiquitously and at high levels. The second most highly expressed serpin gene was OsSRP-PLP (Os11g11500), encoding a non-inhibitory serpin with a surprisingly well-conserved reactive-centre loop (RCL) sequence among putative orthologues in other grass species. Conclusions The diversity of reactive-centre sequences among the putatively inhibitory serpins of rice point to a range of target proteases with different proteolytic specificities. Large differences in basal expression levels of the eight selected rice serpin genes during development further suggest a range of functions in regulation and in plant defence for the corresponding proteins.

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