PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2018 | 87 | 2 |

Tytuł artykułu

Chloroplast protease/chaperone AtDeg2 influences cotyledons opening and reproductive development in Arabidopsis

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
AtDeg2 is a chloroplast protein with dual protease/chaperone activity. Since data on how the individual activities of AtDeg2 affect growth and development of Arabidopsis thaliana plants is missing, two transgenic lines were prepared that express mutated AtDeg2 versions that have either only protease or chaperone activity and a comprehensive ontogenesis stage-based study was performed comprising wild type (WT) plants and insertional mutants that do not express AtDeg2, as well as the two transgenic lines. The repression of both AtDeg2 activities in deg2-3 mutants altered just a few phenotypic traits including the time when cotyledons were fully opened, the time when 10% flowers were open as well as the number of inflorescence branches and seed length in plants which have completed their generative development. It was demonstrated that complete opening of cotyledons as well as the number of inflorescence branches and seed length in plants which have completed their generative development required involvement of both AtDeg2 activities, whereas the time when 10% of flowers were open was controlled by AtDeg2 protease activity. These results show for the first time that the chaperone activity of AtDeg2 is needed for some elements of generative development of A. thaliana plants to proceed normally. So far, the chaperone activity of AtDeg2 was confirmed based on in vitro assays only.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

87

Numer

2

Opis fizyczny

Article 3584 [13p.],fig.,ref.

Twórcy

autor
  • Department of Plant Physiology, Institute of Experimental Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of General Botany, Institute of Experimental Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Biotechnology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Biotechnology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland
autor
  • Department of Plant Physiology, Institute of Experimental Biology, Adam Mickiewicz University in Poznan, Umultowska 89, 61-614 Poznan, Poland

Bibliografia

  • 1. Lipińska B, Sharma S, Georgopoulos C. Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription. Nucleic Acids Res. 1988;16(21):10053–10067. https://doi.org/10.1093/nar/16.21.10053
  • 2. Strauch KL, Beckwith J. An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc Natl Acad Sci USA. 1988;85(5):1576–1580. https://doi.org/10.1073/pnas.85.5.1576
  • 3. Tanz SK, Castleden I, Hooper CM, Small I, Millar AH. Using the SUBcellular database for Arabidopsis proteins to localize the Deg protease family. Front Plant Sci. 2014;5:396. https://doi.org/10.1074/jbc.M108575200
  • 4. Haussühl K, Andersson B, Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J. 2001;20(4):713–722. https://doi.org/10.1093/emboj/20.4.713
  • 5. Sun R, Fan H, Gao F, Lin Y, Zhang L, Gong W, et al. Crystal structure of Arabidopsis Deg2 protein reveals an internal PDZ ligand locking the hexameric resting state. J Biol Chem. 2012;287(44):37564–37569. https://doi.org/10.1074/jbc.M112.394585
  • 6. Jagodzik P, Luciński R, Misztal L, Jackowski G. The contribution of individual domains of chloroplast protein AtDeg2 to its chaperone and proteolytic activities. Acta Soc Bot Pol. 2018;87(1):3570. https://doi.org/10.5586/asbp.3570
  • 7. Stroher E, Dietz KJ. The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. Physiol Plant. 2008;133(3):566–583 https://doi.org/10.1111/j.1399-3054.2008.01103.x
  • 8. Sun XW, Ouyang J, Guo J, Ma J, Lu C Adam Z, et al. The thylakoid protease Deg1 is involved in photosystem-II assembly in Arabidopsis thaliana. Plant J. 2010;62(2):240– 249. https://doi.org/10.1111/j.1365-1313X.2010.04140.x
  • 9. Luciński R, Misztal L, Samardakiewicz S, Jackowski G. The thylakoid protease Deg2 is involved in stress-related degradation of the photosystem II light-harvesting protein Lhcb6 in Arabidopsis thaliana. New Phytol. 2011;192(1):74–86. https://doi.org/10.1111/j.1469-8137.2011.03782.x
  • 10. Jagodzik P, Adamiec M, Jackowski G. AtDeg2 – a chloroplast protein with dual protease/chaperone activity. Acta Soc Bot Pol. 2014;83(3):169–174. https://doi.org/10.5586/asbp.2014.018
  • 11. Baranek M, Wyka T, Jackowski G. Downregulation of chloroplast protease AtDeg5 leads to changes in chronological progression of ontogenetic stages, leaf morphology and chloroplast ultrastructure in Arabidopsis. Acta Soc Bot Pol. 2015:84(1):59–70. https://doi.org/10.5586/asbp.2015.001
  • 12. Earley KW, Haag JR, Pontes O, Opper K, Juehne T, Song K, et al. Gateway-compatible vectors for plant functional genomics and proteomics. Plant J. 2006;45(4):616–629. https://doi.org/10.1111/j.1365-313X.2005.02617.x
  • 13. Grabsztunowicz M, Jackowski G. Isolation of intact and pure chloroplasts form leaves of Arabidopsis thaliana plants acclimated to low irradiance for studies on Rubisco regulation. Acta Soc Bot Pol. 2013;82(1):91–95. https://doi.org/10.5586/asbp.2012.043
  • 14. Lancashire PD, Bleiholder H, van den Boom T, Langelüddeke P, Stauss R, Weber E, et al. A uniform decimal code for growth stages of crops and weeds. Ann Appl Biol. 1991;119:561–560. https://doi.org/10.1111/j.1744-7348.1991.tb04895.x
  • 15. Boyes DC, Zayed AM, Ascenzi R, McCaskill AJ, Hoffman NE, Davis KR, et al. Growth stage-based phenotypic analysis of Arabidopsis: a model for high throughput functional genomics in plants. Plant Cell. 2001;13(7):1499–1510. https://doi.org/10.2307/3871382
  • 16. Kincaid DT, Schneider RB. Quantification of leaf shape with a microcomputer and Fourier transform. Can J Bot. 1983;61:2333–2342. https://doi.org/10.1139/b83-256
  • 17. Western TL, Skinner DJ, Haughn GW. Differentiation of mucilage secretory cells of the Arabidopsis seed coat. Plant Physiol. 2000;122(2):345–356. https://doi.org/10.1104/pp.122.2.345
  • 18. Lobo F, de Barros MP, Dalmagro HJ, Dalmolin ÂC, Pereira WE, de Souza ÉC, et al. Fitting net photosynthetic light-response curves with Microsoft Excel – a critical look at the models. Photosynthetica. 2013;51(3):445–456. https://doi.org/10.1007/s11099-013-0045-y
  • 19. Farquhar GD, von Caemmerer S, Berry JA. A biochemical model of photosynthetic CO² assimilation in leaves of C3 species. Planta. 1980;149(1):78–90. https://doi.org/10.1007/BF00386231
  • 20. Tanaka Y, Sugano SS, Shimada T, Nishimura I. Enhancement of leaf photosynthetic capacity through increased stomatal density in Arabidopsis. New Phytol. 2013;198(3):757–764. https://doi.org/10.1111/nph.12186
  • 21. Long SP, Bernacchi CJ. Gas exchange measurements, what can they tell us about the underlying limitations to photosynthesis? Procedures and sources of error. J Exp Bot. 2003;54(392):2393–2401. https://doi.org/10.1093/jxb/erg262
  • 22. Sharkey TD. What gas exchange data can tell us about photosynthesis. Plant Cell Environ. 2016;39:1161–1163. https://doi.org/10.1111/pce.12641
  • 23. Sjögren LL, Stanne TM, Zheng B, Sutinen S, Clarke AK. Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis. Plant Cell. 2006;18(10):2635–2649. https://doi.org/10.1105/tpc.106.044594
  • 24. Luciński R, Misztal L, Samardakiewicz S, Jackowski G. Involvement of Deg5 proteasae in wounding-related disposal of PsbF apoprotein. Plant Physiol Biochem. 2011;4(3):311– 320. https://doi.org/10.1016/j.plaphy.2011.01.001
  • 25. Kim J, Olinares PD, Oh SH, Ghiasaura S, Poliakov A, Ponnala L, et al. Modified Clp protease complex in ClpP3 null mutant and consequences for chloroplast development and function in Arabidopsis. Plant Physiol. 2013;162(1):157–179. https://doi.org/10.1104/pp.113.215699
  • 26. Xin X, Chen W, Wang B, Zhu F, Li Y, Yang H, et al. Arabidopsis MKK10–MPK6 mediates red-light-regulated opening of seedling cotyledons through phosphorylation of PIF3. J Exp Bot. 2018;69(3):423–439. https://doi.org/10.1093/jxb/erx418
  • 27. Winter D, Vinegar B, Nahal H, Ammar R, Wilson GV, Provart NJ. An “electronic fluorescent pictograph” browser for exploring and analyzing large-scale biological data sets. PLoS One. 2007;2(8):e718. https://doi.org/10.1371/journal.pone.0000718
  • 28. Shrestha R, Gómez-Ariza J, Brambilla V, Fornara F. Molecular control of seasonal flowering in rice, arabidopsis and temperate cereals. Ann Bot. 2014;114(7):1445–1458. https://doi.org/10.1093/aob/mcu032
  • 29. Wu G, Poethig RS. Temporal regulation of shoot development in Arabidopsis thaliana by miR156 and its target SPL3. Development. 2006;133(18):3539–3547. https://doi.org/10.1242/dev.02521
  • 30. Aukerman MJ, Sakai H. Regulation of flowering time and floral organ identity by a microRNA and its APETALA2-like target genes. Plant Cell. 2003;15(11):2730–2741. https://doi.org/10.1105/tpc.016238
  • 31. Liu C, Teo ZW, Bi Y, Song S, Xi W, Yang X, et al. A conserved genetic pathway determines inflorescence architecture in Arabidopsis and rice. Dev Cell. 2013;24(6):612– 622. https://doi.org/10.1016/j.devcel.2013.02.013
  • 32. Han Y, Yiang H, Jiao Y. Regulation of inflorescence architecture by cytokinins. Front Plant Sci. 2014;5:669. https://doi.org/10.3389/fpls.2014.00669
  • 33. Li N, Li Y. Signaling pathways of seed size control in plants. Curr Opin Plant Biol. 2016;33:23–32. https://doi.org/10.1016/j.pbi.2016.05.008

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-34df91e1-a7fc-4e75-89e2-72048a70c404
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.