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2015 | 84 | 1 |

Tytuł artykułu

Identification and expression analysis of a novel phytocystatin in developing and germinating seeds of triticale (x Triticosecale Wittm.)

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
In this paper the complete cDNA sequence of a newly identified triticale phytocystatin, TrcC-7, was analyzed. Because TrcC-7 transcripts were present in seeds, we hypothesized that it may regulate storage protein accumulation and degradation. Therefore, changes in mRNA and protein levels during the entire period of seed development and germination were examined. Expression of TrcC-7 increased during development and decreased at the end of maturation and subsequently increased during seed germination. Based on these results, TrcC-7 likely regulates cysteine proteinase activity during the accumulation and mobilization of storage proteins.

Wydawca

-

Rocznik

Tom

84

Numer

1

Opis fizyczny

p.139-142,fig.,ref.

Twórcy

autor
  • Department of Biochemistry, Faculty of Agriculture and Biology, Warsaw University of Life Sciences - SGGW, Nowoursynowska 159, 02-776 Warsaw, Poland
autor
  • Department of Biochemistry, Faculty of Agriculture and Biology, Warsaw University of Life Sciences - SGGW, Nowoursynowska 159, 02-776 Warsaw, Poland

Bibliografia

  • 1. Grudkowska M, Zagdańska B. Multifunctional role of plant cysteine proteinases. Acta Biochim Polon. 2004;51:609–624.
  • 2. Szewińska J, Zdunek-Zastocka E, Pojmaj M, Bielawski W. Molecular cloning and expression analysis of triticale phytocystatins duringdevelopment and germination of seeds. Plant Mol Biol Rep.2012;30:867–877. http://dx.doi.org/10.1007/s11105-011-0384-4
  • 3. Prabucka B, Drzymała A, Grabowska A. Molecular cloning and expression analysis of the main gliadin-degrading cysteine endopeptidaseEP8 from triticale. J Cereal Sci. 2013;58:284–289. http://dx.doi.org/10.1016/j.jcs.2013.06.004
  • 4. Szewińska J, Prabucka B, Krawczyk M, Mielecki M, Bielawski W. The participation of phytocystatin TrcC-4 in the activity regulation of EP8, the main prolamin degrading cysteine endopeptidase in triticale seeds. Plant Growth Regul. 2013;69:131–137. http://dx.doi. org/10.1007/s10725-012-9756-5
  • 5. Chomczynski P, Sacchi N. Single-step method of total RNA isolation by acid guanidinium thiocyanate-phenol-chloroformextraction. Anal Biochem. 1987;162:156–159. http://dx.doi.org/10.1016/0003-2697(87)90021-2
  • 6. Untergrasser A, Cutcutache I, Koressaar T, Ye J, Faircloth BC, Remm M, Rozen SG. Primer3 – new capabilities and interfaces. NucleicAcids Res. 2012;40(15):e115. http://dx.doi.org/10.1093/nar/gks596
  • 7. Katoh K, Standley DM. MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Mol Biol Evol.2013;30:772–780. http://dx.doi.org/10.1093/molbev/mst010
  • 8. Goujon M, McWilliam H, Li W, Valentin F, Squizzato S, Paern J, Lopez R. A new bioinformatics analysis tools framework at EMBLEBI.Nucleic Acids Res. 2010;38(2 suppl):W695–W699. http://dx.doi.org/10.1093/nar/gkq313
  • 9. Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASyserver. In: Walker JM, editor. The proteomics protocols handbook.New York, NY: Humana Press; 2005. p. 571–607. http://dx.doi.org/10.1385/1-59259-890-0:571
  • 10. Petersen TN, Brunak S, von Heijne G, Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods.2011;8:785–786. http://dx.doi.org/10.1038/nmeth.1701
  • 11. Martinez M, Cambra I, Carrillo L, Diaz-Mendoza M, Diaz I. Characterization of the entire cystatin gene family in barley and their targetcathepsin L-like cysteine-proteases, partners in the hordein mobilizationduring seed germination. Plant Physiol. 2009;151:1531–1545.http://dx.doi.org/10.1104/pp.109.146019
  • 12. Abe K, Emori Y, Kondo H, Suzuki K, Arai S. Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology withanimal cystatins and transient expression in the ripening process ofrice seeds. J Biol Chem. 1987;262:16793–16797.
  • 13. Kondo H, Abe K, Nishimura I, Watanabe H, Emori Y, Arai S. Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II. J Biol Chem. 1990;265:15832–15837.
  • 14. Massonneau A, Condamine P, Wisniewski JP, Zivy M, Rogowsky PM. Maize cystatins respond to developmental cues, cold stress anddrought. Biochim Biophys Acta. 2005;1729:186–199. http://dx.doi.org/10.1016/j.bbaexp.2005.05.004
  • 15. Corre-Menguy F, Cejudo FJ, Mazubert C, Vidal J, Lelandais-Brière C, Torres G, Rode A, Hartmann C. Characterization of the expressionof a wheat cystatin gene during caryopsis development. Plant MolBiol. 2002;50:687–698. http://dx.doi.org/10.1023/A:1019906031305
  • 16. Kuroda M, Kiyosaki T, Matsumoto I, Misaka T, Arai S, Abe K. Molecular cloning, characterization, and expression of wheat cystatins. Biosci Biotechnol Biochem. 2001;65:22–28. http://dx.doi.org/10.1271/bbb.65.22
  • 17. Abraham Z, Martinez M, Carbonero P, Diaz I. Structural and functional diversity within the cystatin gene family of Hordeum vulgare.J Exp Bot. 2006;57:4245–4255. http://dx.doi.org/10.1093/jxb/erl200
  • 18. Dutt S, Singh VK, Marla SS, Kumar A. In silico analysis of sequential, structural and functional diversity of wheat cystatins and itsimplication in plant defense. Genomics Proteomics Bioinformatics.2010;8:42–56. http://dx.doi.org/10.1016/S1672-0229(10)60005-8
  • 19. Womack JS, Randall J, Kemp JD. Identifcation of a signal peptide for oryzacystatin-I. Planta. 2000;210:844–847. http://dx.doi.org/10.1007/s004250050688

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-2ca4cd58-7781-4d80-ba8d-4e721f5c6684
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