Relevant bibliographies by topics / Catalabolisme de la proline

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Catalabolisme de la proline'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Catalabolisme de la proline"

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Sarhan, S., and N. Seiler. "Proline and proline derivatives as anticonvulsants." General Pharmacology: The Vascular System 20, no. 1 (January 1989): 53–60. http://dx.doi.org/10.1016/0306-3623(89)90060-8.

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Myung, Sunnie, Maren Pink, Mu-Hyun Baik, and David E. Clemmer. "DL-Proline." Acta Crystallographica Section C Crystal Structure Communications 61, no. 8 (July 23, 2005): o506—o508. http://dx.doi.org/10.1107/s0108270105021001.

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Opalka, Suzanne M., Ashley R. Longstreet, and D. Tyler McQuade. "Continuous proline catalysis via leaching of solid proline." Beilstein Journal of Organic Chemistry 7 (December 14, 2011): 1671–79. http://dx.doi.org/10.3762/bjoc.7.197.

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Herein, we demonstrate that a homogeneous catalyst can be prepared continuously via reaction with a packed-bed of a catalyst precursor. Specifically, we perform continuous proline catalyzed α-aminoxylations using a packed-bed of L-proline. The system relies on a multistep sequence in which an aldehyde and thiourea additive are passed through a column of solid proline, presumably forming a soluble oxazolidinone intermediate. This transports a catalytic amount of proline from the packed-bed into the reactor coil for subsequent combination with a solution of nitrosobenzene, affording the desired optically active α-aminooxy alcohol after reduction. To our knowledge, this is the first example in which a homogeneous catalyst is produced continuously using a packed-bed. We predict that the method will not only be useful for other L-proline catalyzed reactions, but we also foresee that it could be used to produce other catalytic species in flow.
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Gruttadauria, Michelangelo, Francesco Giacalone, and Renato Noto. "Supported proline and proline-derivatives as recyclable organocatalysts." Chemical Society Reviews 37, no. 8 (2008): 1666. http://dx.doi.org/10.1039/b800704g.

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Csaba, G., and P. Kovács. "Imprinting Effects of Proline Containing Dipeptides (Proline-Glycine, Proline-Leucine, Proline-Valine and Their Retro Variants) in Tetrahymena. Evolutionary Conclusions." Bioscience Reports 17, no. 6 (December 1, 1997): 537–42. http://dx.doi.org/10.1023/a:1027360207238.

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Proline-glycine, proline-leucine and proline-valine dipeptides and their retro variants were used in the experiments to study the effects of pretreatment (imprinting) in Tetrahymena, by investigating fluorescein isothiocyanate (FITC)-conjugated peptide binding. The protozoan organism could differentiate between the proline-dipeptides containing different partner amino-acids and between the dipeptides having the amino acids in reversed positions. The effect of imprinting was positive or negative and this was dependent on the type of the partner amino acid and on its position. Pro-Gly and Pro-Leu induced positive imprinting (elevated FITC-dipeptide binding) and Pro-Val induced negative imprinting (decrease of FITC-peptide binding). There was positive imprinting induction in two cases for the retro FITC-peptide and in one case for the FITC-conjugate of the imprinter peptide itself. The highest positive imprinting (almost 60% increase) was induced by Pro-Gly for FITC-Gly-Pro. Considering earlier—chemotaxis—experiments, the results of the present—binding—studies run parallel with the physiological effects. The experiments call attention to the sharp differentiating ability of small peptides at a unicellular level, that could have some role in the selection of molecules for hormone formation, during evolution.
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Rutella, Giuseppina Sefora, Lisa Solieri, Serena Martini, and Davide Tagliazucchi. "Release of the Antihypertensive Tripeptides Valine-Proline-Proline and Isoleucine-Proline-Proline from Bovine Milk Caseins during in Vitro Gastrointestinal Digestion." Journal of Agricultural and Food Chemistry 64, no. 45 (November 7, 2016): 8509–15. http://dx.doi.org/10.1021/acs.jafc.6b03271.

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Medha, Sadhna Sharma, and Monika Sharma. "Proline-Glutamate/Proline-Proline-Glutamate (PE/PPE) proteins of Mycobacterium tuberculosis: The multifaceted immune-modulators." Acta Tropica 222 (October 2021): 106035. http://dx.doi.org/10.1016/j.actatropica.2021.106035.

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Mandalapu, Dhanaraju. "l-Proline and d-Proline (Chiral Amino Acid Catalysts)." Synlett 26, no. 05 (February 19, 2015): 707–8. http://dx.doi.org/10.1055/s-0034-1380270.

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Tritsch, Denis, Hiba Mawlawi, and Jean-François Biellmann. "Mechanism-based inhibition of proline dehydrogenase by proline analogues." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1202, no. 1 (September 1993): 77–81. http://dx.doi.org/10.1016/0167-4838(93)90065-y.

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Hill, JeffW, and EdwinM Nemoto. "N -acetyl proline-glycine-proline: implications for neurological disorders." Neural Regeneration Research 11, no. 6 (2016): 0. http://dx.doi.org/10.4103/1673-5374.184478.

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Dissertations / Theses on the topic "Catalabolisme de la proline"

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Zheng, Yao. "Identification of interacting mitochondrial enzymes involved in pyrroline-5-carboxylate metabolism in Arabidopsis thaliana." Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS269.pdf.

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La proline, acide aminé protéinogène, joue un rôle crucial dans le métabolisme cellulaire. Dans les mitochondries, la proline est oxydée en glutamate par l'action séquentielle de la proline déshydrogénase (ProDH) et de la pyrroline-5-carboxylate (P5C) déshydrogénase (P5CDH). L'ornithine-δ-aminotransférase (δOAT) participe également à la formation de P5C via la conversion de l'ornithine et de l’α -cétoglutarate en glutamate et P5C. L’utilisation de mutants et d’approches biochimiques a révélé que ProDH1, P5CDH et δOAT sont impliquées dans la sénescence des feuilles induite à l'obscurité (DIS) chez Arabidopsis thaliana. Une accumulation importante de P5C et de proline est observée chez le mutant p5cdh et, dans une moindre mesure chez le mutant prodh1prodh2, suggérant un cycle proline-P5C. Les mutants prodh1prodh2 et p5cdh ont un profil métabolomique similaire qui diffère de celui du WT et de oat, démontrant ainsi le rôle de l'oxydation de la proline au cours de la sénescence. Nous avons montré que ProDH1 est essentiellement associée à la membrane mitochondriale, tandis que P5CDH et δOAT sont plus uniformément réparties entre la matrice et la membrane. L’oligomérisation de ProDH1, P5CDH et δOAT a été révélée à l'aide d’une analyse de complémentation bimoléculaire de fluorescence (BiFC). Les interactions entre ces enzymes du métabolisme du P5C ont été confirmées par des approches de protéomique couplée à la MS en condition de sénescence chez A. thaliana. Ces trois enzymes forment un(des) complexe(s) impliqué(s) dans l'oxydation de la proline pour alimenter la chaîne de transfert d'électrons mitochondriale afin de pourvoir aux besoins énergétiques des cellules sénescentes
The proteinogenic amino acid proline plays a crucial role for cellular metabolism in living organisms. In mitochondria, proline is oxidized to glutamate by the sequential action of proline dehydrogenase (ProDH) and pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH). In addition, ornithine δ-aminotransferase (δOAT) also participates in P5C formation through the conversion of ornithine and α-ketoglutarate into glutamate and P5C. Using mutants and biochemical approaches, ProDH1, P5CDH and δOAT were shown to be involved during dark-induced leaf senescence (DIS) in Arabidopsis thaliana. Striking accumulation of P5C and proline was observed in p5cdh mutant and to a lesser extent in prodh1prodh2 mutant, suggesting a putative proline-P5C cycle. Metabolomic analysis indicated that prodh1prodh2 and p5cdh have a similar metabolomic profile, but significantly different from wild-type and oat mutant, demonstrating the role of proline oxidation during DIS. ProDH1 was shown to be preferentially associated to the mitochondrial membrane fraction, while P5CDH and δOAT are more evenly distributed between matrix and membrane fractions. Homo- and hetero-oligomerizations of ProDH1, P5CDH, and δOAT were revealed using Bimolecular Fluorescence Complementation (BiFC) assay of infiltrated tobacco leaves. Interactions between P5C metabolism enzymes were further highlighted in DIS leaves using proteomics approaches coupled with mass spectrometry. Our work demonstrates that these three enzymes form P5C metabolic complex(es) involved in the oxidation of proline to fuel mitochondrial electron transfer chain to support the energy needs of senescent cells
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Hsueh, Li-Ching. "Studies on proline hydroxylases." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365805.

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Küllchen, Felix B. "Studies on proline 3-hydroxylase." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.269221.

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Schulz, Daniel [Verfasser]. "L-Proline and Glutamatergic Neurotransmission : Clarifying the Modulatory Role of Neuronal L-Proline Transporter / Daniel Schulz." Bonn : Universitäts- und Landesbibliothek Bonn, 2012. http://d-nb.info/1044971096/34.

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Lawrence, Christopher C. "Studies on bacterial proline 4-hydroxylase." Thesis, University of Oxford, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358610.

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Hu, Chien-an Andy. "Osmoregulation and proline biosynthesis in plants /." The Ohio State University, 1993. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487843688956923.

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Townsend, David E. Wilkinson Brian J. "Proline transport and biosynthesis in Staphylococcus aureus." Normal, Ill. Illinois State University, 1992. http://wwwlib.umi.com/cr/ilstu/fullcit?p9311291.

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Thesis (Ph. D.)--Illinois State University, 1992.
Title from title page screen, viewed February 6, 2006. Dissertation Committee: Brian J. Wilkinson (chair), Radheshyam Jayaswal, Herman E. Brockman, Robert L. Preston, Philip D. Morse. Includes bibliographical references (leaves 107-112) and abstract. Also available in print.
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Le, Dinh Thien. "Métabolisme de la proline chez les mammifères." Paris 5, 1988. http://www.theses.fr/1988PA05P216.

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Habibi-Najafi, Mohammad B. (Mohammad Bagher). "Proline-specific peptidases from Lactobacillus casei subspecies." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=28455.

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The objectives of this study were (l) to screen out active proline-specific peptidases from Lactobacillus casei subspecies, (2) to study growth kinetic and enzyme production from enriched medium (MRS) and cheese whey medium, (3) to purify and characterize two active proline-specific enzymes, and (4) to investigate the action of purified enzyme on bitter tryptic digests of $ beta$-casein as well as bitter enzyme-modified cheese. Lactobacillus casei subsp. casei LLG and Lactobacillus casei subsp. rhamnosus S93 were examined for extra- and intra-cellular proline-specific peptidase activities. Both strains showed strong activity for x-prolyl dipeptidyl peptidase and proline iminopeptidase but had weak activities for prolidase, prolinase, and post proline endopeptidase. Histochemical staining of crude enzyme extract from Lactobacillus casei ssp. casei LLG with different substrates revealed a distinct protein band for x-prolyl dipeptidyl peptidase as well as for proline iminopeptidase. The growth kinetics showed that the intracellular proline-specific peptidases increased gradually at the beginning of the exponential phase and reached a maximum at the beginning of stationary phase.
Storage stability of x-prolyl dipeptidyl peptidase and proline iminopeptidase in crude extract, with and without stabilizers showed no significant loss in activity of these two enzymes at 4$ sp circ$C for 9 days without adding any stabilizers. The levels of x-prolyl dipeptidyl peptidase, proline iminopeptidase, and post proline endopeptidase activities of cells grown in whey did not vary markedly from cells grown in MRS broth. X-prolyl dipeptidyl peptidase and proline iminopeptidase were purified from crude cell-free extract of Lactobacillus casei ssp. casei LLG by Fast Protein Liquid Chromatography (FPLC) equipped with ion-exchange and gel-filtration columns. X-prolyl dipeptidyl peptidase was found to be a serine-dependent enzyme with molecular mass of 79 kDa. The pH and the temperature optima by the purified enzyme were 7.0 and 50$ sp circ$C, respectively. Proline iminopeptidase was sulfhydryl enzyme with molecular mass of 46 kDa. The maximum enzyme activity was observed at pH 7.5 and 40$ sp circ$C. This is the first report describing the purification and characterization of x-prolyl dipeptidyl peptidase and proline iminopeptidase from Lactobacillus casei to homogeneity.
The debittering of tryptic digests from $ beta$-casein by x-prolyl dipeptidyl peptidase was studied by reversed phase high performance liquid chromatography (RP-HPLC) and liquid chromatography/mass spectrometry. The results showed that two bitter peptides (f53-97 and f03-209) containing X-Pro-Y-Pro in their amino acid residues were completely hydrolyzed and many other peptides with high hydrophobicity were decreased in peak area. The addition of purified x-prolyl dipeptidyl peptidase on bitter enzyme-modified cheese (EMC) also showed that at least one bitter peptide with X-Pro-Y derived from $ alpha$-casein hydrolysis was removed.
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Walters, Nicola Jane. "Arginine and proline catabolism in Schizosaccharomyces pombe." Thesis, University of Cambridge, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.257192.

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Books on the topic "Catalabolisme de la proline"

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Sorrell, Barbara Jane. Conformation of proline residues in bacteriorhodopsin. Ottawa: National Library of Canada, 1990.

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Wood, Nicholas James. The role of proline in osmoregulation by a streptomycete. [s.l.]: typescript, 1996.

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Clymer Toro proline hydrostatic commercial walk-behind mowers, 1990 & later. Overland Park, Kan: Primedia, 2003.

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Drzymala, Lukasz. Phosphorylation of human salivary proline-rich proteins in cultured cells. Ottawa: National Library of Canada, 1998.

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Chan, Maggie Tin Lai. Proteolytic processing of recombinant human salivary proline-rich protein precursors (PRPs). Ottawa: National Library of Canada, 2000.

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Chan, John Chi Cheong. Purification and characterization of recombinant human basic proline-rich protien precursor. Ottawa: National Library of Canada, 1996.

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Blankenstein, Petra. Isolierung, Charakterisierung und Lokalisierung der Prolylhydroxylase aus Chlamydomonas reinhardii und Daucus carota. Konstanz: Hartung-Gorre, 1988.

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Spielman, Andrew I. Purification and characterization of the proline-rich proteins from rabbit parotid saliva. [Toronto: University of Toronto, Faculty of Dentistry], 1988.

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Lu, Ying. Characterization of the interaction of human salivary proline-rich proteins with tannins. [Toronto: University of Toronto, Faculty of Dentistry], 1997.

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Shen, Lixin. The Influence of microwave heating on the rate of racemization of L-proline. Sudbury, Ont: Laurentian University, 1993.

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Book chapters on the topic "Catalabolisme de la proline"

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Kobayashi, Kensei. "Proline." In Encyclopedia of Astrobiology, 1344. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1282.

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Kobayashi, Kensei. "Proline." In Encyclopedia of Astrobiology, 2025. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1282.

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Sapse, Anne-Marie. "Proline." In Molecular Orbital Calculations for Amino Acids and Peptides, 63–73. Boston, MA: Birkhäuser Boston, 2000. http://dx.doi.org/10.1007/978-1-4612-1354-3_6.

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Kobayashi, Kensei. "Proline." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1282-4.

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Kobayashi, Kensei. "Proline." In Encyclopedia of Astrobiology, 2470. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1282.

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Zhang, Shilei, and Wei Wang. "Proline Derivatives." In Privileged Chiral Ligands and Catalysts, 409–45. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527635207.ch11.

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Schomburg, D., M. Salzmann, and D. Stephan. "Proline dehydrogenase." In Enzyme Handbook 7, 203–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_42.

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Hirota, E., K. Kuchitsu, T. Steimle, J. Vogt, and N. Vogt. "28 C5H9NO2 Proline." In Molecules Containing Three or Four Carbon Atoms and Molecules Containing Five or More Carbon Atoms, 192. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-41504-3_159.

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Schomburg, Dietmar, and Dörte Stephan. "Procollagen-proline dioxygenase." In Enzyme Handbook, 271–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-57942-4_57.

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Demaison, J. "557 C5H9NO2 Proline." In Asymmetric Top Molecules. Part 2, 519–21. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-10400-8_305.

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Conference papers on the topic "Catalabolisme de la proline"

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Hlaváček, Jan, Jan Mařík, Blanka Bennettová, and Richard Tykva. "Proline-rich peptides." In VIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199903061.

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Xu, X., PL Jackson, S. Tanner, M. Hardison, JE Blalock, and A. Gaggar. "Acetylated Proline-Glycine-Proline (Ac-PGP) and Interleukin-8 Induce MMP-9 Release from Neutrophils." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3717.

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Moravčíková, Daniela, Dušan Berkeš, and Anna Koreňová. "Synthesis of Conformationally Restricted Proline Chimeras." In The 16th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2012. http://dx.doi.org/10.3390/ecsoc-16-01056.

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Carrillo Fernández, Luisa, Jose Luis Vicario, Iker Riaño, Estibaliz Diaz, Efraim Reyes Martín, and Uxue Uria. "Enantioselective Synthesis of Chiral Proline Derivatives." In MOL2NET 2016, International Conference on Multidisciplinary Sciences, 2nd edition. Basel, Switzerland: MDPI, 2016. http://dx.doi.org/10.3390/mol2net-02-h004.

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Ten, Galina N., and Natalia E. Shcherbakova. "Proline tautomerism in the solid phase." In Laser Physics, Photonic Technologies, and Molecular Modeling, edited by Vladimir L. Derbov. SPIE, 2022. http://dx.doi.org/10.1117/12.2625832.

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CARVALHO, Gustavo Almeida de, Ricardo Cambraia PARREIRA, Onésia Cristina Oliveira LIMA, Elis Marra da Madeira FREITAS, Bruno Lemes MARQUES, Thiago Gonçalves BARBOSA, Flávio Silva de CARVALHO, et al. "Proline transporter inhibitor affects Swiss mice behavior." In Anais do I Congresso Internacional de Farmacologia Molecular Aplicada. Recife, Brasil: Even3, 2019. http://dx.doi.org/10.29327/16216.1-3.

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Inforzato, Tatiane, Liane Marcia Rossi, Tiago Venancio, and Alcindo A. Dos Santos. "Silica-Supported Proline Derivatives for Catalytic Studies." In 14th Brazilian Meeting on Organic Synthesis. São Paulo: Editora Edgard Blücher, 2013. http://dx.doi.org/10.5151/chempro-14bmos-r0201-1.

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Abdurashytova, E. R., S. F. Abdurashytov, and E. E. Turin. "Influence of biopreparations on the content of proline and chlorophyll Sorghum bicolor L. in Steppe conditions." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.006.

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The use of biopreparations on sorghum contributed to a 38.2% increase in proline and 1.4 times more yields in a dry year, and in a favorable year, seed pre-sowing inoculation reduced the concentration of proline (by 49.8%) and chlorophyll (by 6.5%).
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Motrich, Artem, Roman Besaga, Iryna Soltys, Mykhailo Slyotov, and Olexander V. Galochkin. "Determination of proline concentration in natural biological environments." In Fourteenth International Conference on Correlation Optics, edited by Oleg V. Angelsky. SPIE, 2020. http://dx.doi.org/10.1117/12.2553902.

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Hancock, Chad N., and James Phang. "Abstract 1119: The oxidation of proline by proline oxidase provides a regulated source of ROS for mitochondria derived cellular signaling." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1119.

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Reports on the topic "Catalabolisme de la proline"

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Sergiev, Iskren, Dessislava Todorova, and Lyubomira Atanasova. High Salinityinduced Proline and Polyamine Changes in Organs of Pea (Pisum sativumL. Cv. Ran). "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, November 2018. http://dx.doi.org/10.7546/crabs.2018.11.06.

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Taub, Floyd E., and Richard E. Weller. Proline-Rich Polypeptide 1 and GX-NH2: Molecular and Genetic Mechanisms of Hematopoiesis Regulation. Office of Scientific and Technical Information (OSTI), September 2011. http://dx.doi.org/10.2172/1025686.

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Zilberstein, Aviah, Bo Liu, and Einat Sadot. Studying the Involvement of the Linker Protein CWLP and its Homologue in Cytoskeleton-plasma Membrane-cell Wall Continuum and in Drought Tolerance. United States Department of Agriculture, June 2012. http://dx.doi.org/10.32747/2012.7593387.bard.

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The study has been focused on proline-rich proteins from the HyPRP family. Three proline-rich proteins have been characterized with the CWLP as the main objective. We showed that this unique protein is assembled in the plasma membrane (PM) and forms a continuum between the cell wall (CW) and cytosol via the PM. While spanning the PM, it is arranged in lipid rafts as CWLP-aquaporin complexes that recruit PP2A-β”, as a part of PP2A enzyme, close to the aquaporin moiety where it dephosphorylates two crucial Ser residues and induces closure of the aquaporin water channels. The closure of water channels renders cells more tolerant to plasmolysis and plants to dehydration. This unique effect was observed not only in Arabidopsis, but also in potato plants over expressing the CWLP, suggesting a possible usage in crop plants as a valve that reduces loss of water or/and elevates cold resistance. The CWLP is a member of the HyPRP protein family that all possess structurally similar 8CM domain, predicted to localize to PM lipid rafts. In this study, two additional highly homologous HyPRP proteins were also studied. The GPRP showed the same localization and it’s over expression increased tolerance to lack of water. However, the third one, PRP940, despite sharing high homology in the 8CM domain, is completely different and is assembled in parallel to cortical microtubules in the cell. Moreover, our data suggest that this protein is not involved in rendering plants resistant to lack of water. We suggest implying CWLP as a tool for better regulation of water maintenance in crop plants.
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Bray, Elizabeth, Zvi Lerner, and Alexander Poljakoff-Mayber. The Role of Phytohormones in the Response of Plants to Salinity Stress. United States Department of Agriculture, September 1994. http://dx.doi.org/10.32747/1994.7613007.bard.

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Salinity is an increasing problem in many irrigated areas of crop production and is a significant factor in reducing crop productivity. Developmental, physiological, and molecular responses to salinity were studied in order to improve our understanding of these responses. Improvements in our understanding of plant responses to salinity are necessary in order to develop crops with improved salt tolerance. Previously, in Israel, it was shown that Sorghum biccolor can adapt to an otherwise lethal concentration of NaCl. These experiments were refined and it was shown that there is a specific window of development in which this adaption can occur. Past the window of development, Sorghum plants can not be adapted. In addition, the ability to adapt is not present in all genotypes of Sorghum. Cultivars that adapt have an increased coefficient of variation for many of the physiological parameters measured during the mid-phase of adaptation. Therefore, it is possible that the adaptation process does not occur identically in the entire population. A novel gene was identified, isolated and characterized from Sorghum that is induced in roots in response to salinity. This gene is expressed in roots in response to salt treatments, but it is not salt-induced in leaves. In leaves, the gene is expressed without a salt treatment. The gene encodes a proline-rich protein with a novel proline repeat, PEPK, repeated more than 50 times. An antibody produced to the PEPK repeat was used to show that the PEPK protein is present in the endodermal cell wall of the root during salt treatments. In the leaves, the protein is also found predominantly in the cell wall and is present mainly in the mesophyll cells. It is proposed that this protein is involved in the maintenance of solute concentration.
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Lers, Amnon, Majid R. Foolad, and Haya Friedman. genetic basis for postharvest chilling tolerance in tomato fruit. United States Department of Agriculture, January 2014. http://dx.doi.org/10.32747/2014.7600014.bard.

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ABSTRACT Postharvest losses of fresh produce are estimated globally to be around 30%. Reducing these losses is considered a major solution to ensure global food security. Storage at low temperatures is an efficient practice to prolong postharvest performance of crops with minimal negative impact on produce quality or human health and the environment. However, many fresh produce commodities are susceptible to chilling temperatures, and the application of cold storage is limited as it would cause physiological chilling injury (CI) leading to reduced produce quality. Further, the primary CI becomes a preferred site for pathogens leading to decay and massive produce losses. Thus, chilling sensitive crops should be stored at higher minimal temperatures, which curtails their marketing life and in some cases necessitates the use of other storage strategies. Development of new knowledge about the biological basis for chilling tolerance in fruits and vegetables should allow development of both new varieties more tolerant to cold, and more efficient postharvest storage treatments and storage conditions. In order to improve the agricultural performance of modern crop varieties, including tomato, there is great potential in introgression of marker-defined genomic regions from wild species onto the background of elite breeding lines. To exploit this potential for improving tomato fruit chilling tolerance during postharvest storage, we have used in this research a recombinant inbred line (RIL) population derived from a cross between the red-fruited tomato wild species SolanumpimpinellifoliumL. accession LA2093 and an advanced Solanum lycopersicumL. tomato breeding line NCEBR-1, developed in the laboratory of the US co-PI. The original specific objectives were: 1) Screening of RIL population resulting from the cross NCEBR1 X LA2093 for fruit chilling response during postharvest storage and estimation of its heritability; 2) Perform a transcriptopmic and bioinformatics analysis for the two parental lines following exposure to chilling storage. During the course of the project, we learned that we could measure greater differences in chilling responses among specific RILs compared to that observed between the two parental lines, and thus we decided not to perform transcriptomic analysis and instead invest our efforts more on characterization of the RILs. Performing the transcriptomic analysis for several RILs, which significantly differ in their chilling tolerance/sensitivity, at a later stage could result with more significant insights. The RIL population, (172 lines), was used in field experiment in which fruits were examined for chilling sensitivity by determining CI severity. Following the field experiments, including 4 harvest days and CI measurements, two extreme tails of the response distribution, each consisting of 11 RILs exhibiting either high sensitivity or tolerance to chilling stress, were identified and were further examined for chilling response in greenhouse experiments. Across the RILs, we found significant (P < 0.01) correlation between field and greenhouse grown plants in fruit CI. Two groups of 5 RILs, whose fruits exhibited reproducible chilling tolerant/sensitive phenotypes in both field and greenhouse experiments, were selected for further analyses. Numerous genetic, physiological, biochemical and molecular variations were investigated in response to postharvest chilling stress in the selected RILs. We confirmed the differential response of the parental lines of the RIL population to chilling stress, and examined the extent of variation in the RIL population in response to chilling treatment. We determined parameters which would be useful for further characterization of chilling response in the RIL population. These included chlorophyll fluorescence Fv/Fm, water loss, total non-enzymatic potential of antioxidant activity, ascorbate and proline content, and expression of LeCBF1 gene, known to be associated with cold acclimation. These parameters could be used in continuation studies for the identification and genetic mapping of loci contributing to chilling tolerance in this population, and identifying genetic markers associated with chilling tolerance in tomato. Once genetic markers associated with chilling tolerance are identified, the trait could be transferred to different genetic background via marker-assisted selection (MAS) and breeding. The collaborative research established in this program has resulted in new information and insights in this area of research and the collaboration will be continued to obtain further insights into the genetic, molecular biology and physiology of postharvest chilling tolerance in tomato fruit. The US Co-PI, developed the RIL population that was used for screening and measurement of the relevant chilling stress responses and conducted statistical analyses of the data. Because we were not able to grow the RIL population under field conditions in two successive generations, we could not estimate heritability of response to chilling temperatures. However, we plan to continue the research, grow the RIL progeny in the field again, and determine heritability of chilling tolerance in a near future. The IS and US investigators interacted regularly and plan to continue and expand on this study, since combing the expertise of the Co-PI in genetics and breeding with that of the PI in postharvest physiology and molecular biology will have great impact on this line of research, given the significant findings of this one-year feasibility project.
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