Academic literature on the topic 'Plant Peptide Hormones'
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Journal articles on the topic "Plant Peptide Hormones"
Motomitsu, Ayane, Shinichiro Sawa, and Takashi Ishida. "Plant peptide hormone signalling." Essays in Biochemistry 58 (September 15, 2015): 115–31. http://dx.doi.org/10.1042/bse0580115.
Full textKaufmann, Christine, and Margret Sauter. "Sulfated plant peptide hormones." Journal of Experimental Botany 70, no. 16 (June 20, 2019): 4267–77. http://dx.doi.org/10.1093/jxb/erz292.
Full textGancheva, M. S., Yu V. Malovichko, L. O. Poliushkevich, I. E. Dodueva, and L. A. Lutova. "Plant Peptide Hormones." Russian Journal of Plant Physiology 66, no. 2 (March 2019): 171–89. http://dx.doi.org/10.1134/s1021443719010072.
Full textMatsushima, Norio, Hiroki Miyashita, Shinsuke Tamaki, and Robert H. Kretsinger. "Polyproline II Helix as a Recognition Motif of Plant Peptide Hormones and Flagellin Peptide flg22." Protein & Peptide Letters 26, no. 9 (September 16, 2019): 684–90. http://dx.doi.org/10.2174/0929866526666190408125441.
Full textHsiao, Yu-Chun, and Masashi Yamada. "The Roles of Peptide Hormones and Their Receptors during Plant Root Development." Genes 12, no. 1 (December 25, 2020): 22. http://dx.doi.org/10.3390/genes12010022.
Full textMatsubayashi, Yoshikatsu, and Youji Sakagami. "PEPTIDE HORMONES IN PLANTS." Annual Review of Plant Biology 57, no. 1 (June 2006): 649–74. http://dx.doi.org/10.1146/annurev.arplant.56.032604.144204.
Full textHirakawa, Yuki, Keiko U. Torii, and Naoyuki Uchida. "Mechanisms and Strategies Shaping Plant Peptide Hormones." Plant and Cell Physiology 58, no. 8 (May 10, 2017): 1313–18. http://dx.doi.org/10.1093/pcp/pcx069.
Full textJeon, Byeong Wook, Min-Jung Kim, Shashank K. Pandey, Eunkyoo Oh, Pil Joon Seo, and Jungmook Kim. "Recent advances in peptide signaling during Arabidopsis root development." Journal of Experimental Botany 72, no. 8 (February 17, 2021): 2889–902. http://dx.doi.org/10.1093/jxb/erab050.
Full textGermain, Hugo, Eric Chevalier, and Daniel P. Matton. "Plant bioactive peptides: an expanding class of signaling molecules." Canadian Journal of Botany 84, no. 1 (January 2006): 1–19. http://dx.doi.org/10.1139/b05-162.
Full textYamada, Masashi, and Shinichiro Sawa. "The roles of peptide hormones during plant root development." Current Opinion in Plant Biology 16, no. 1 (February 2013): 56–61. http://dx.doi.org/10.1016/j.pbi.2012.11.004.
Full textDissertations / Theses on the topic "Plant Peptide Hormones"
Bastian, René. "Characterisation of AtPNP-A - a novel arabidopsis thaliana gene with role in water and salt homeostasis." Thesis, University of the Western Cape, 2009. http://hdl.handle.net/11394/2818.
Full textPlant natriuretic peptides (PNPs) are a novel class of extracellular, systemically mobile molecules that elicit a number of plant responses important in homeostasis and growth. Natriuretic peptides were first identified in vertebrates where they play a role in the regulation of salt and water balance. Subsequent experimental investigations have identified the presence of a natriuretic peptide hormone system in plants. While PNPs have been implicated in various physiological responses such as stomatal guard cell movements and regulation of net water uptake, its biological role has remained elusive. Here we have used co-expression and promoter content analysis tools to understand the biological role of the Arabidopsis thaliana PNP (AtPNP-A). The analysis of AtPNP-A and its co-expressed genes revealed that genes annotated as part of the systemic acquired resistance (SAR) pathway were over-represented, thus suggesting that AtPNP-A may function as a component of plant defense responses and specifically, SAR. The results further show that AtPNP-A shares many characteristics with pathogenesis related (PR) proteins in that its transcription is strongly induced in response to pathogen challenges, thus implying a newly described role for AtPNP-A in pathogen attack. Additional tissue expression analysis also indicated distinct localization of PNP activity in sepals and transcriptional meta-analysis showed that AtPNP-A may play a role in starch breakdown. Therefore, together with the finding that AtPNP-A plays a role in regulating phloem transport, we also hypothesize that AtPNP-A may play a role in phloem unloading in sepals to assist processes such as seed formation in plants. In plants, the second messenger, guanosine 3’,5’-cyclic monophosphate (cGMP) mediates a whole range of important processes including salinity tolerance, disease resistance, drought tolerance and responses to light. Since PNPs regulate water and salt homeostasis via a cGMP-dependent signaling pathways, it is thus important to analyse the transcriptome induced by the second messenger (cGMP) in Arabidopsis thaliana to give a better understanding of its mechanism of action. This study was also supplemented by the analysis of the gibberellic acid (GA) dependent transcriptome, since cGMP also plays a role its transcription pathway. This data analysis, together with promoter content investigation, revealed that genes upregulated after cGMP treatment and down-regulated in the GA insensitive mutant (ga1-3) were enriched with a GA response element (GARE), while no GARE enrichment were observed in genes up-regulated in the ga1-3 mutant. These findings suggest that GARE is indicative of GA-induced and cGMP-dependent transcriptional up-regulation. Gene ontology analysis confirmed previous reports that cGMP is involved in ion homeostasis and indicated that the transcriptional cGMP response is bi-polar in the sense that both genes up- and down-regulated in response to cGMP is involved in cation transport. Additionally, ab initio analysis of genes transcriptionally dependent on cGMP identified CHX8 as a hub gene and promoter content of CHX8 co-expressed genes show enrichment of the GARE motif. The fact that CHX8 has its highest expression levels during male gametogenesis and pollen tube growth, together with our findings, suggest that GA-induced and cGMP- dependent genes may play a key role in ion and water homeostasis in the male gametophyte. Finally, we propose that the type of analysis undertaken here can yield new insights into gene regulation networks and inform experimental strategies to unravel complex transcription regulatory systems under different developmental and stimulus specific conditions.
South Africa
Hove, Runyararo Memory. "Evolutionary development and functional role of plant natriuretic peptide (PNP)-B." Thesis, University of Fort Hare, 2009. http://hdl.handle.net/10353/155.
Full textPharmawati, Made, and mikewood@deakin edu au. "A study of the natriuretic peptide hormone system in plants." Deakin University. School of Biological and Chemical Sciences, 1999. http://tux.lib.deakin.edu.au./adt-VDU/public/adt-VDU20060727.145040.
Full textFiori, Celso Spada. "Identificação e caracterização de componentes da via de transdução de sinais do peptídeo hormonal RALF." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-20102010-111024/.
Full textThe peptide hormone research has begun during the 90s decade with the systemin discovery. Nowadays several peptides have already been identified, and some of them are further characterized. The involvement of these molecules with a range of basic and specific biological functions has raised the scientific communitys interest. Among the peptides being studied, the RALF family is particularly intriguing. The RALF peptides can be found throughout the plant kingdom, from the moss Physcomitrella patens to the mono and dicot plant groups. The conserved occurrence of these peptides along the plant kingdom suggests an important role in the plant physiology field. Recent evidences indicate that RALF plays a role in basic mechanisms of plant development. The RALF mechanism of action and its perception by the cell are fundamental information in order to characterize this peptide function. In the present work experiments to identify RALF interacting proteins were employed. The results indicate that RALF peptides activity is possibly regulated by the calcium ion. This regulation is mediated by the interaction with a calcium binding protein. This calcium binding protein was found to be secreted to the apoplast. Presented data suggests that RALF is regulated by a mechanism never described before in the plant hormone research field. As previously described in animals and yeast the RALF propeptide processing takes place in a dibasic site. A single amino acid site specific mutation disrupted peptide processing in vivo and in vitro. The correct processing is mediated by proteases of the Arabidopsis microsomal fraction. This processing seems to occur at the endomembrane system, possibly catalized by a convertase class enzyme. The published results points the beginning of the peptide processing studies in plants.
Abad, Juan Carlos Guerrero. "Identificação da subtilase responsável pelo processamento do prepopeptídeo AtRALF1 em Arabidopsis thaliana." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-09022012-162000/.
Full textSince the 90s, a new family of molecules of protein origin and with hormone characteristics has been studied in plants. This group of new molecules, collectively named peptide hormones, is involved in defense, reproduction, growth and development. RALF, one of these peptides, is ubiquitous in plants and is involved in plant development. In Arabidopsis there are 34 RALF-like genes (AtRALFs). Our group has shown that AtRALF1 is processed from a larger precursor by a subtilase. Arabidopsis has 56 subtilases, our goal is the identification of the specific subtilase that is responsible for the AtRALF1 processing. Prediction of subcelular localization and in silico gene expression analysis, both confirmed by RT-PCR expression analysis and chimeric proteins with green-fluorescent protein, allowed the reduction of the initial 56 candidates to only 7 subtilases. Crosses between knockout mutants or RNAi plants expressing low levels of subtilases with overexpressors of AtRALF1 identified the subtilases AtSBT6.1 (At5g19660) and AtSBT5.3 (At2g04160) as potentialy involved in the prepropeptide AtRALF1 processing.
Ruzvidzo, Oziniel. "Plant Natriuretic Peptides - Elucidation of the Mechanisms of Action." Thesis, University of the Western Cape, 2009. http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_5854_1285860491.
Full textSeveral lines of cellular and physiological evidence have suggested the presence of a novel class of systemically mobile plant molecules that are recognized by antibodies generated against vertebrate atrial natriuretic peptides (ANPs). Functional characterization of these immunoanalogues, referred to as immunoreactive plant natriuretic peptides (irPNPs) or plant natriuretic peptides (PNPs), has shown that they play important roles in a number of cellular processes crucial for plant growth and maintenance of cellular homeostasis. Although the various biological roles of PNPs in plants are known, their exact mode of action remains elusive. To elucidate the mechanisms of action for these immunoanalogues, we have prepared a biologically active recombinant PNP from Arabidopsis thaliana (AtPNP-A) and the biological activity was demonstrated by showing its ability to induce water uptake into Arabidopsis thaliana protoplasts. In addition, the molecule was shown to downregulate photosynthesis while at the same time up-regulating respiration, transpiration as well as net water uptake and retention capacities in the sage Plectranthus ecklonii. Further analysis of the recombinant AtPNP-A indicated that the peptide can induce systemic response signalling though the phloem. A recombinant Arabidopsis wall associated kinase-like protein (AtWAKL10) that has a domain organization resembling that of vertebrate natriuretic peptide (NP) receptors was also partially characterized as a possible receptor for the recombinant AtPNP-A. Vertebrate NP receptors contain an extracellular ligand-binding domain and an intracellular guanylate cyclase (GC)/kinase domain and signal through the activity of their GC domain that is capable of generating intracellular cGMP from GTP. The structural resemblance of AtWAKL10 to vertebrate NP receptors could suggest a functional homology with receptor molecules and it is conceivable that such a receptor may recognize PNPs as ligands. The characterization of the recombinant AtWAKL10 showed that the molecule functions as both a GC and a kinase in vitro. This strengthened the suggestion that AtWAKL10 could be a possible AtPNP-A receptor especially considering the fact that AtPNP-A applications to plant cells also
trigger cGMP transients. Furthermore, a bioinformatic analysis of the functions of AtPNP-A and AtWAKL10 has inferred both molecules in plant pathogen responses and defense mechanisms, thus indirectly functionally linking the two proteins.
Norberg, Åke. "Isolation and characterization of regulatory peptides and bioactive compounds /." Stockholm : Karolinska institutet, 2004. http://diss.kib.ki.se/2004/91-7349-882-3/.
Full textSugano, Shigeo S. "Identification of stomagen, a novel plant peptide hormone, and its function in stomatal development." 京都大学 (Kyoto University), 2013. http://hdl.handle.net/2433/175154.
Full textBergonci, Tábata. "Análise funcional dos peptídeos RALF em Arabidopsis: avaliação do efeito do hormônio brassinolide em plantas superexpressoras e silenciadas para os genes AtRALF1 e AtRALF34." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/11/11144/tde-29052012-104800/.
Full textLike in animals, plant peptide hormones play important roles in growth, development and defense. RALF is a peptide hormone ubiquitous in plants that was first isolated from tobacco leaves. Although its function has not been established, the information gathered so far suggest its involvement with basic aspects of cellular biology, probably cellular elongation. RALF peptides in Arabidopsis are found in a multigene family of 37 members. Transgenic plants overexpressing AtRALF1 under the control of the strong constitutive promoter 35S, show a semi-dwarf phenotype and root growth inhibition. A similar phenotype was also observed when AtRALF23 was overexpressed. AtRALF23, as opposed to AtRALF1, is inhibited by brassinosteroids. These facts suggest that different RALF peptide hormones, despite the convergence to the same function, show a unique relationship with other hormones. The goal of this work was to contribute to the determination of the function of RALF peptides in plants and to clarify the inter-relationship between RALF and the other plant hormones. With that in mind, the isoforms AtRALF1 and AtRALF34 were selected based on primary structure similarity/dissimilarity and pattern of gene expression. Plants with high levels of expression or silenced for both genes were obtained and evaluated. The gene construct AtRALF1-GFP was introduced in Arabidopsis under the control of the 35S promoter and fluorescence was observed in the endoplasmic reticulum, Golgi apparatus and apoplast. Genes previously reported as induced in 35S:AtRALF1 plants were validated and used in AtRALF1 peptide and brassinolide experiments. Taken together our results suggest an antagonistic effect of the peptide AtRALF1 regarding the elongation effect of brassinolide in hypocotyls and roots. Plants with high levels of AtRALF1 are resistant to exogenously applied brassinolide, and do not show typical responses to the steroid hormone. The antagonism between the two hormones was also suggested by the gene expression analysis of the AtRALF1 and brassinolide inducible genes.
Mingossi, Fabiana Bombonato. "Análise da expressão gênica dos peptídeos hormonais RALF em cana-de-açúcar." Universidade de São Paulo, 2009. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-14042009-082857/.
Full textRapid Alkalinization Factor (RALF) is part of a growing family of peptides with hormone characteristics in plants. Initially isolated from leaves of tobacco plants, RALF peptides can be found throughout the plant kingdom and they are expressed in plants ubiquitously. Sugarcane plants have four isoforms of SacRALF genes and SacRALF1 isoform is expressed predominantly. SacRALF1 transcripts are abundant in the elongation zone of root tips and all four SacRALF genes are more expressed in young and expanding leaves than in expanded leaves. In leaf blades, SacRALF gene transcripts were found at high levels at the basal portion of the leaf and at low levels at the apical portion. The whole set of gene expression analyses showed in this study, suggest that SacRALF genes expression is localized in elongation zones of roots and leaves. Mature leaves that are devoid of elongating cells do not show considerable expression of SacRALF genes. Sugarcane embryogenic cell suspension cultures showed a nearly constitutive level of SacRALF gene transcripts. SacRALF1 peptide was added to culture media and inhibited the growth of microcalli derived from cell suspension cultures at concentrations as low as 0.1 µM. Microcalli exposed to exogenous SacRALF1 showed a reduced number of elongated cells. The findings suggest that RALF peptides have a role in plant development, particularly in cell elongation.
Books on the topic "Plant Peptide Hormones"
Patisaul, Heather B., and Scott M. Belcher. The Neuroendocrine System and General Mechanisms of Endocrine Disruption. Oxford University Press, 2017. http://dx.doi.org/10.1093/acprof:oso/9780199935734.003.0004.
Full textBurton, Derek, and Margaret Burton. Food procurement and processing. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780198785552.003.0004.
Full textBook chapters on the topic "Plant Peptide Hormones"
Ryan, Clarence A., and Gregory Pearce. "Peptide Hormones for Defense, Growth, Development and Reproduction." In Plant Hormones, 700–716. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-1-4020-2686-7_30.
Full textWang, Jizong, Guangzhong Lin, Rui Ma, Zhifu Han, and Jijie Chai. "Structural Insight into Recognition of Plant Peptide Hormones by Plant Receptor Kinases." In Plant Structural Biology: Hormonal Regulations, 31–46. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-91352-0_3.
Full textMiliner, P. A., D. A. Groarke, and I. R. White. "Synthetic peptides as probes of plant cell signalling." In Plant Hormone Signal Perception and Transduction, 217–21. Dordrecht: Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-0131-5_29.
Full textSpecht, T., G. Slosarek, H. R. Kalbitzer, V. A. Erdmann, M. Giel-Pietraszuk, M. Szymanski, P. Mucha, P. Rekowski, G. Kupryszewski, and J. Barciszewski. "The Tertiary Structure of Plant Peptide Hormone Systemin and the Mechanism of its Action." In Plant Proteins from European Crops, 41–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-03720-1_7.
Full textHofmann, Alexander, Alexander Minges, and Georg Groth. "Interfering Peptides Targeting Protein–Protein Interactions in the Ethylene Plant Hormone Signaling Pathway as Tools to Delay Plant Senescence." In Methods in Molecular Biology, 71–85. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0954-5_7.
Full textSong, Xiu-Fen, Shi-Chao Ren, and Chun-Ming Liu. "Peptide hormones." In Hormone Metabolism and Signaling in Plants, 361–404. Elsevier, 2017. http://dx.doi.org/10.1016/b978-0-12-811562-6.00011-6.
Full textDalton, David R. "Roots, Shoots, Leaves, and Grapes." In The Chemistry of Wine. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780190687199.003.0015.
Full textConference papers on the topic "Plant Peptide Hormones"
Gancheva, M. S., E. A. Rutkovskaya, L. O. Polyushkevich, M. A. Lebedeva, I. E. Dodueva, and L. A. Lutova. "Peptide hormones CLE and CEP in potatoes." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-112.
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