Chloroplast protease/chaperone AtDeg2 influences cotyledons opening and reproductive development in Arabidopsis
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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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
DOI: https://doi.org/10.5586/asbp.3584
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