Abstract
The chloroplast is a typical plant organelle in plant cells, which is mainly responsible for photosynthesis as well as other essential functions. The chloroplast has gained considerable attention due to its intricate biochemical pathways for indispensable metabolite functions. New technologies, in combination with increasing amounts of plant genome data, have opened up experimental possibilities to identify a more complete set of chloroplast proteins (the chloroplast proteome), both the whole chloroplast and its main subcellular compartments. A great effort has been made to study chloroplast proteome changes under abiotic stresses for better understanding of photosynthesis and identifying the stress-responsive proteins. Abiotic stress is likely to cause a reduction in CO2 fixation and lead to the forming of excess reactive oxygen species (ROS) that impair the functions of chloroplast proteins involved in photosynthesis. In this chapter, we summarize recent significant achievements in research on chloroplast proteome changes under abiotic stress, hoping to provide insights on the intrinsic mechanism of abiotic stress response in plants.
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References
Bruley C, Dupierris V, Salvi D et al (2012) AT_CHLORO: A chloroplast protein database dedicated to sub-plastidial localization. Front Plant Sci 3(4):279–286
Saravanavel R, Ranganathan R, Anantharaman P (2011) Effect of sodium chloride on photosynthetic pigments and photosynthetic characteristics of Avicennia officinalis seedlings. Recent Res Sci Technol 3(4):177–180
Uberegui E, Hall M, Lorenzo Ó et al (2015) An Arabidopsis soluble chloroplast proteomic analysis reveals the participation of the Executer pathway in response to increased light conditions. J Exp Bot 66(7):2067–2077
Ashraf M, Harris PJC (2013) Photosynthesis under stressful environments: An overview. Photosynthetica 51(2):163–190
Agrawal GK, Bourguignon J, Rolland N et al (2011) Plant organelle proteomics: collaborating for optimal cell function. Mass Spectrom Rev 30(5):772–853
van Wijk KJ, Baginsky S (2011) Plastid proteomics in higher plants: current state and future goals. Plant Physiol 155(4):1578–1588
Leister D (2003) Chloroplast research in the genomic age. Trends Genet 19(1):47–56
Ferro M, Brugière S, Salvi D et al (2010) AT_CHLORO: A comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol Cell Proteomics 9(6):1063–1084
Zybailov B, Rutschow H, Friso G et al (2008) Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 3(4):e1994
Lundquist PK, Poliakov A, Bhuiyan NH et al (2012) The functional network of the Arabidopsis plastoglobule proteome based on quantitative proteomics and genomewide coexpression analysis. Plant Physiol 158(3):1172–1192
Sun QZB, Majeran W, Friso G et al (2009) PPDB, the plant proteomics database at cornell. Nucleic Acids Res 37(Database issue): 969–974
Heazlewood JL, Verboom RE, Tonti-Filippini J et al (2007) SUBA: the Arabidopsis Subcellular Database. Nucleic Acids Res 35(suppl 1):213–218
Kleffmann T, Hirschhoffmann M, Gruissem W et al (2006) Plprot: A comprehensive proteome database for different plastid types. Plant Cell Physiol 47(3):432–436
Joshi HJ, Hirsch-Hoffmann M, Baerenfaller K et al (2011) MASCP Gator: an aggregation portal for the visualization of Arabidopsis proteomics data. Plant Physiol 155(1):259–270
Goksoyr J (1967) Evolution of eucaryotic cells. Nature 214(5093):1161
Jarvis P, Soll J (2001) Toc, Tic, and chloroplast protein import. BBA-MOL Cell Res 1541 (s 1–2): 64–79
Rahnama A, Poustini K, Tavakkol-Afshari R et al (2010) Growth and stomatal responses of bread wheat genotypes in tolerance to salt stress. Int J Biol Life Sci 6(4):216–221
Medici LO, Azevedo RA, Canellas LP et al (2007) Stomatal conductance of maize under water and nitrogen deficits. Pesquisa Agropecuária Brasileira 42(4):599–601
Chaves MM, Flexas J, Pinheiro C (2009) Photosynthesis under drought and salt stress: regulation mechanisms from whole plant to cell. Ann Bot-London 103(4):551–560
Kosmala A, Perlikowski D, Pawłowicz I et al (2012) Changes in the chloroplast proteome following water deficit and subsequent watering in a high- and a low-drought-tolerant genotype of Festuca arundinacea. J Exp Bot 63(17):6161–6172
Galvez-Valdivieso G, Mullineaux PM (2010) The role of reactive oxygen species in signalling from chloroplasts to the nucleus. Physiol Plantarum 138(4):430–439
Rinalducci S, Murgiano L, Zolla L (2008) Redox proteomics: basic principles and future perspectives for the detection of protein oxidation in plants. J Exp Bot 59(14):3781–3801
Caruso G, Cavaliere C, Guarino C et al (2008) Identification of changes in Triticum durum L. Leaf proteome in response to salt stress by two-dimensional electrophoresis and MALDI-TOF mass spectrome try. Anal Bioanal Chem 391(1):381–390
Zörb C, Herbst R, Forreiter C et al (2009) Short-term effects of salt exposure on the maize chloroplast protein pattern. Proteomics 9(17):4209–4220
Aghaei K, Ehsanpour AA, Shah AH et al (2009) Proteome analysis of soybean hypocotyl and root under salt stress. Amino Acids 36(1):91–98
Hu X, Wu X, Li C et al (2012) Abscisic acid refines the synthesis of chloroplast proteins in maize (Zea mays) in response to drought and light. PLoS ONE 7(11):488
Kamal AH, Cho K, Choi JS et al (2013) The wheat chloroplastic proteome. J Proteomics 93(19):326–342
Kamal AH, Cho K, Kim DE et al (2012) Changes in physiology and protein abundance in salt-stressed wheat chloroplasts. Mol Biol Rep 39(9):9059–9074
Wang R, Chen S, Deng L et al (2007) Leaf photosynthesis, luorescence response to salinity and the relevance to chloroplast salt compartmentation and anti-oxidative stress in two poplars. Trees-Struct Func 21(5):581–591
Kamal AH, Cho K, Choi JS et al (2012) Patterns of protein expression in water-stressed wheat chloroplasts. Biol Plant 57(2):305–312
Wang D, Luthe DS (2003) Heat sensitivity in a bentgrass variant. Failure to accumulate a chloroplast heat shock protein isoform implicated in heat tolerance. Plant Physiol 133(1):319–327
Kim KH, Alam I, Kim YG et al (2012) Overexpression of a chloroplast-localized small heat shock protein OsHSP26 confers enhanced tolerance against oxidative and heat stresses in tall fescue. Biotechnol Lett 34(2):371–377
Hu X, Yang Y, Gong F et al (2015) Protein sHSP26 improves chloroplast performance under heat stress by interacting with specific chloroplast proteins in maize (Zea mays). J Proteomics 115:81–92
Schafer G, Kardinahl S (2003) Iron superoxide dismutases: structure and function of an archaic enzyme. Biochem Soc T 31(6):1130–1134
Khanna-Chopra R, Jajoo A, Semwal VK (2012) Chloroplasts and mitochondria have multiple heat tolerant isozymes of SOD and APX in leaf and inflorescence in Chenopodium album. Biochem Bioph Res Co 412(4):522–525
Sainz M, DÃaz P, Monza J et al (2010) Heat stress results in loss of chloroplast Cu/Zn superoxide diasmutase and increased damage to Photosystem II in combined drought-heat stressed Lotus japonicas. Physiol Plant 140(1):46–56
Ruelland E, Vaultier MN, Zachowski A et al (2009) Cold signalling and cold acclimation in plants. Adv Bot Res 49:35–150
Goulas E, Schubert M, Kieselbach T et al (2006) The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short-and long-term exposure to low temperature. Plant J 47(5):720–734
Reiland S, Messerli G, Baerenfaller K et al (2009) Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks. Plant Physiol 150(2):889–903
Kupsch C, Ruwe H, Gusewski S et al (2012) Arabidopsis chloroplast RNA binding proteins CP31A and CP29A associate with large transcript pools and confer cold stress tolerance by influencing multiple chloroplast RNA processing steps. Plant Cell 24(10):4266–4280
Kirchhoff H (2014) Structural changes of the thylakoid membrane network induced by high light stress in plant chloroplasts. Philos T Roy Soc 369(1640):1925–1953
Lintala M, Allahverdiyeva Y, Kangasjärvi S (2009) Comparative analysis of leaf-type ferredoxin-NADP+ oxidoreductase isoforms in Arabidopsis thaliana. Plant J 57(6):1103–1115
Buchert F, Forreiter C (2010) Singlet oxygen inhibits ATPase and proton translocation activity of the thylakoid ATP synthase CF1CFo. FEBS Lett 584(1):147–152
Buchert F, Schober Y (2012) Römpp a reactive oxygen species affect ATP hydrolysis by targeting a highly conserved amino acid cluster in the thylakoid ATP synthase γ subunit. BBA-Bioenergetics 1817(1):2038–2048
Kohzuma K, Dal Bosco C, Meurer J (2013) Light- and metabolism-related regulation of the chloroplast ATP synthase has distinct mechanisms and functions. J Biol Chem 288(18):13156–13163
Giacomelli L, Rudella A, van Wijk KJ (2006) High light response of the thylakoid proteome in Arabidopsis wild type and the ascorbate-deficient mutant vtc2-2 A comparative proteomics study. Plant Physiol 141(2):685–701
Dühring U, Irrgang KD, Lunser K et al (2006) Analysis of photosynthetic complexes from a cyanobacterial ycf37 mutant. BBA-Bioenergetics 1757(1):3–11
Ranieri A, Giuntini D, Ferraro F et al (2001) Chronic ozone fumigation induces alterations in thylakoid functionality and composition in two poplar clones. Plant Physiol Bioch 39(11):999–1008
Ahsan N, Nanjo Y, Sawada H et al (2010) Ozone stress-induced proteomic changes in leaf total soluble and chloroplast proteins of soybean reveal that carbon allocation is involved in adaptation in the early developmental stage. Proteomics 10(14):2605–2619
Bohler S, Bagard M, Oufir M et al (2007) A DIGE analysis of developing poplar leaves subjected to ozone reveals major changes in carbon metabolism. Proteomics 7(10):1584–1599
Bohler S, Sergeant K, Hoffmann L et al (2011) A difference gel electrophoresis study on thylakoids isolated from poplar leaves reveals a negative impact of ozone exposure on membrane proteins. J Proteome Res 10(7):3003–3011
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Ning, F., Wang, W. (2016). The Response of Chloroplast Proteome to Abiotic Stress. In: Hossain, M., Wani, S., Bhattacharjee, S., Burritt, D., Tran, LS. (eds) Drought Stress Tolerance in Plants, Vol 2. Springer, Cham. https://doi.org/10.1007/978-3-319-32423-4_9
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DOI: https://doi.org/10.1007/978-3-319-32423-4_9
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