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Relevant bibliographies by topics / Proline-rich

Academic literature on the topic 'Proline-rich'

Author: Grafiati

Published: 11 March 2023

Last updated: 1 April 2023

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Journal articles on the topic "Proline-rich"

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Schlundt, Andreas, Jana Sticht, Kirill Piotukh, Daniela Kosslick, Nadin Jahnke, Sandro Keller, Michael Schuemann, Eberhard Krause, and Christian Freund. "Proline-rich Sequence Recognition." Molecular & Cellular Proteomics 8, no. 11 (June 20, 2009): 2474–86. http://dx.doi.org/10.1074/mcp.m800337-mcp200.

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Kofler, Michael, Michael Schuemann, Christian Merz, Daniela Kosslick, Andreas Schlundt, Astrid Tannert, Michael Schaefer, Reinhard Lührmann, Eberhard Krause, and Christian Freund. "Proline-rich Sequence Recognition." Molecular & Cellular Proteomics 8, no. 11 (May 30, 2009): 2461–73. http://dx.doi.org/10.1074/mcp.m900191-mcp200.

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Mishra, Awdhesh, Jaehyuk Choi, Eunpyo Moon, and Kwang-Hyun Baek. "Tryptophan-Rich and Proline-Rich Antimicrobial Peptides." Molecules 23, no. 4 (April 2, 2018): 815. http://dx.doi.org/10.3390/molecules23040815.

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Stahl, L. E., R. L. Wright, J. D. Castle, and A. M. Castle. "The unique proline-rich domain of parotid proline-rich proteins functions in secretory sorting." Journal of Cell Science 109, no. 6 (June 1, 1996): 1637–45. http://dx.doi.org/10.1242/jcs.109.6.1637.

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When expressed in pituitary AtT-20 cells, parotid proline-rich proteins enter the regulated pathway. Because the short N-terminal domain of a basic proline-rich protein is necessary for efficient export from the ER, it has not been possible to evaluate the role of this polypeptide segment as a sorting signal for regulated secretion. We now show that addition of the six-amino acid propeptide of proparathyroid hormone to the proline-rich protein, and especially to a deletion mutant lacking the N-terminal domain, dramatically accelerates intracellular transport of these polypeptides. Under these conditions the chimeric deletion mutant is stored as effectively as the full-length protein in dense core granules. The propeptide does not function as a sorting signal in AtT-20 cells as it does not reroute a constitutively secreted reporter protein to the regulated pathway. During transit, the propeptide is cleaved from the chimeric polypeptides such that the original structures of the full-length and the deletion mutant proline-rich proteins are reestablished. We have also found that the percentage stimulated secretion of the proline-rich proteins increases incrementally (almost twofold) as their level of expression is elevated. The increase reflects an enrichment of these polypeptides in the granule pool and its incremental nature suggests that sorting of proline-rich proteins involves an aggregation-based process. Because we can now rule out contributions to sorting by both N- and C-terminal segments of the proline-rich protein, we deduce that the unique proline-rich domain is responsible for storage. Thus at least some of the determinants of sorting for regulated secretion are protein-specific rather than universal.

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Seifert, Trevor B., Arnold S. Bleiweis, and L. Jeannine Brady. "Contribution of the Alanine-Rich Region of Streptococcus mutans P1 to Antigenicity, Surface Expression, and Interaction with the Proline-Rich Repeat Domain." Infection and Immunity 72, no. 8 (August 2004): 4699–706. http://dx.doi.org/10.1128/iai.72.8.4699-4706.2004.

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ABSTRACT Streptococcus mutans is considered to be the major etiologic agent of human dental caries. Attachment of S. mutans to the tooth surface is required for the development of caries and is mediated, in part, by the 185-kDa surface protein variously known as antigen I/II, PAc, and P1. Such proteins are expressed by nearly all species of oral streptococci. Characteristics of P1 include an alanine-rich repeat region and a centrally located proline-rich repeat region. The proline-rich region of P1 has been shown to be important for the translational stability and translocation of P1 through the bacterial membrane. We show here that (i) several anti-P1 monoclonal antibodies require the simultaneous presence of the alanine-rich and proline-rich regions for binding, (ii) the proline-rich region of P1 interacts with the alanine-rich region, (iii) like the proline-rich region, the alanine-rich region is required for the stability and translocation of P1, (iv) both the proline-rich and alanine-rich regions are required for secretion of P1 in Escherichia coli, and (v) in E. coli, P1 is secreted in the absence of SecB.

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Robinson, R., D. L. Kauffman, M. M. Y. Waye, M. Blum, A. Bennick, and P. J. Keller. "Primary structure and possible origin of the non-glycosylated basic proline-rich protein of human submandibular/sublingual saliva." Biochemical Journal 263, no. 2 (October 15, 1989): 497–503. http://dx.doi.org/10.1042/bj2630497.

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Human submandibular/sublingual saliva contains one non-glycosylated basic proline-rich protein whereas parotid saliva contains multiple such components. The submandibular protein has a primary structure identical with the C-terminal segment [TZ] of the human parotid acidic proline-rich proteins that contain 150 amino acid residues (Mr 16,000). Northern-blot analyses of human parotid and submandibular glands revealed that mRNAs containing the HaeIII repeat sequence typical for acidic proline-rich proteins are expressed in both of these salivary glands whereas mRNAs for non-glycosylated basic proline-rich proteins containing a typical BstN1 repeat sequence are expressed in the parotid but not in the submandibular gland. Products of translation in vitro of mRNAs from human parotid and submandibular glands were also examined. Two immunoprecipitable bands with Mr 29,000 and 28,000 were obtained by translation of both parotid and submandibular mRNA. In the presence of microsomal membranes these proteins gave rise to proteins electrophoretically identical with the secreted acidic proline-rich proteins of Mr 16,000. These proteins were cleaved by kallikrein, giving rise to proteins with electrophoretic mobilities identical with those of a smaller acidic proline-rich protein with Mr 11,000 and peptide TZ. Additional immunoprecipitable bands with Mr ranging from 35,000 to 46,000 were seen when parotid mRNA was used for translation in vitro, and are believed to be precursors of the basic proline-rich proteins encoded by the BstN1 repeat type mRNA. Neither these bands nor a separate precursor for the basic non-glycosylated proline-rich protein was detected when submandibular mRNA was used for translation in vitro. It is suggested that the non-glycosylated basic proline-rich protein present in human submandibular saliva arises by cleavage of acidic proline-rich proteins.

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OHBA, Takeaki, Masaho ISHINO, Hiroshi AOTO, and Terukatsu SASAKI. "Interaction of two proline-rich sequences of cell adhesion kinase β with SH3 domains of p130Cas-related proteins and a GTPase-activating protein, Graf." Biochemical Journal 330, no. 3 (March 15, 1998): 1249–54. http://dx.doi.org/10.1042/bj3301249.

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Cell adhesion kinase β (CAKβ) is a protein tyrosine kinase closely related to focal adhesion kinase (FAK) in structure. CAKβ contains two proline-rich sequences within its C-terminal region. Since proline-rich sequences present in the corresponding region of FAK are known to mediate protein-protein interactions by binding to SH3 domains, we investigated binding of CAKβ to a panel of SH3 domains. Affinity precipitation from rat brain lysate revealed selective interactions of CAKβ with glutathione S-transferase (GST)-fused SH3 domains of p130Cas(Cas)-related proteins and Graf. Mutational analysis indicated that the proline-rich sequences of CAKβ mediate this interaction. Each of the two proline-rich sequences fused to GST bound directly to these SH3 domains in dot blot analysis. A competitive binding assay revealed that the first proline-rich sequence of CAKβ preferentially associated with the SH3 domain of Cas. The second proline-rich sequence of CAKβ bound to the SH3 domain of Graf with higher specificity than the corresponding proline-rich sequence of FAK. Finally, we showed co-immunoprecipitation of CAKβ with Graf from rat brain lysate. These results indicate that CAKβ associates in vivo with Graf through its SH3 domain.

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Bezirganyan, Kristina B., Tigran K. Davtyan, and Armen A. Galoyan. "Hypothalamic Proline Rich Polypeptide Regulates Hematopoiesis." Neurochemical Research 35, no. 6 (December 18, 2009): 917–24. http://dx.doi.org/10.1007/s11064-009-0109-3.

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Pujals, Sílvia, and Ernest Giralt. "Proline-rich, amphipathic cell-penetrating peptides." Advanced Drug Delivery Reviews 60, no. 4-5 (March 2008): 473–84. http://dx.doi.org/10.1016/j.addr.2007.09.012.

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Luck, Genevieve, Hua Liao, Nicola J. Murray, Heidi R. Grimmer, Edward E. Warminski, Michael P. Williamson, Terence H. Lilley, and Edwin Haslam. "Polyphenols, astringency and proline-rich proteins." Phytochemistry 37, no. 2 (January 1994): 357–71. http://dx.doi.org/10.1016/0031-9422(94)85061-5.

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Dissertations / Theses on the topic "Proline-rich"

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Dikic, Inga. "Signal Transduction by Proline-Rich Tyrosine Kinase Pyk2." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2002. http://publications.uu.se/theses/91-554-5316-3/.

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Bess, Kirstin. "Transcriptional repression by the proline rich homeodomain protein." Thesis, University of Bristol, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.390994.

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Murray, Nicola Jane. "NMR studies of salivary proline-rich proteins and tannins." Thesis, University of Sheffield, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284595.

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Swingler, Tracey. "Transcriptional repression by the proline rich homeodomain protein (PRH)." Thesis, University of Bristol, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.419215.

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Drzymala, Luke. "Phosphorylation of human salivary proline-rich proteins in cultured cells." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0001/MQ40692.pdf.

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Soufi, Abdenour. "Oligomerisation and phosphorylation of the proline-rich homeodomain protein (PRH)." Thesis, University of Bristol, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.432944.

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Chan, Maggie Tin Lai. "Proteolytic processing of recombinant human salivary proline-rich protein precursors (PRPs)." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0025/MQ50333.pdf.

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Kofler, Michael. "GYF domains a class of proline rich ligand binding adaptor domains /." kostenfrei, 2007. http://www.diss.fu-berlin.de/2007/261/index.html.

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Lu, Ying. "Characterization of the interaction of human salivary proline-rich proteins with tannins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq29245.pdf.

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Charlton, Adrian Jon. "Study of the interaction between salivary proline-rich proteins and plant polyphenols." Thesis, University of Sheffield, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.327666.

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Books on the topic "Proline-rich"

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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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4

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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6

Spielman, Andrew I. Purification and partial characterization of two proline-rich proteins from rabbit parotid saliva. [Toronto: Faculty of Dentistry], University of Toronto, 1985.

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Charlton, Bernard. Cloning and characterization of Drosophila Nedd4 as a putative binding partner of the proline-rich region of Inscuteable. Ottawa: National Library of Canada, 1999.

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8

Dikic, Inga. Signal Transduction by Proline-Rich Tyrosine Kinase Pyk2. Uppsala Universitet, 2002.

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9

Spielman, Andrei Ioan. Purification and characterization of the proline-rich proteins from rabbit parotid saliva. 1988.

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10

Hemschoote, K. Characterisation of an Androgen-Regulated Mrna Encoding Multiple Proline-Rich Polypeptides in the Rat Ventral Prostrate. Leuven University Press, 1989.

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Book chapters on the topic "Proline-rich"

1

Farrera-Sinfreu, Josep, Ernest Giralt, Miriam Royo, and Fernando Albericio. "Cell-Penetrating Proline-Rich Peptidomimetics." In Peptide Characterization and Application Protocols, 241–67. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-430-8_9.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Proline-Rich Tyrosine Kinase 1." In Encyclopedia of Signaling Molecules, 1478. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101093.

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Dempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, Yuan Xiao Zhu, A. Keith Stewart, Jaime O. Claudio, Constance E. Runyan, et al. "SH3 Domain–Containing Proline-Rich Kinase." In Encyclopedia of Signaling Molecules, 1729. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101236.

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Freund, C., H. G. Schmalz, J. Sticht, and R. Kühne. "Proline-Rich Sequence Recognition Domains (PRD): Ligands, Function and Inhibition." In Handbook of Experimental Pharmacology, 407–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-72843-6_17.

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Gibbons, R. J., and D. I. Hay. "Adsorbed Salivary Proline-Rich Proteins as Bacterial Receptors on Apatitic Surfaces." In Molecular Mechanisms of Microbial Adhesion, 143–63. New York, NY: Springer New York, 1989. http://dx.doi.org/10.1007/978-1-4612-3590-3_12.

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Otvos, Laszlo, Goran Kragol, Gyorgyi Varadi, Barry A. Condie, and Sandor Lovas. "The Proline-Rich Antibacterial Peptide Family Inhibits Chaperone-Assisted Protein Folding." In Peptides: The Wave of the Future, 873–75. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_408.

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Sommerfeldt, D. W., M. Priemel, T. Schinke, S. Mansour, M. Amling, and J. M. Rueger. "»Proline-rich transcript of the brain« beeinflusst die Knochenmasse in vivo." In Deutsche Gesellschaft für Chirurgie, 379–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18547-2_115.

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Azen, Edwin A., and Lang Zhuo. "Molecular-Genetic Studies of Mouse Proline-Rich Protein Genes and Bitter Taste." In Olfaction and Taste XI, 231–32. Tokyo: Springer Japan, 1994. http://dx.doi.org/10.1007/978-4-431-68355-1_88.

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Baraldi, Elena, Maria Macias, Marko Hyvonen, Hartmut Oschkinat, and Matti Saraste. "Spectroscopical studies on the interaction between ww domain and proline-rich peptides." In Interacting Protein Domains, 45–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60848-3_7.

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Otvos, Laszlo Jr, Marco Cassone, Vanessa de Olivier Inacio, Paul Noto, John J. Rux, John D. Wade, and Predrag Cudic. "Synergy Between a Lead Proline-rich Antibacterial Peptide Derivative and Small Molecule Antibiotics." In Advances in Experimental Medicine and Biology, 375–78. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_165.

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Conference papers on the topic "Proline-rich"

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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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Jayaraman, PS, KY Lee, P. Kitchen, D. Clark, J. Lertsuwan, A. Sawasdichai, S. Oltean, J. Satayavivad, SA Simon Afford, and K. Gaston. "PO-120 Proline rich homeodomain protein is required for cholangiocarcinoma tumour growth." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.161.

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Koide, T. "CHARACTERIZATION OF THE GENE FOR HUMAN HISTIDINE-RICH GLYCOPROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643599.

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Human histidine-rich glycoprotein (HRG) is a single-chain glycoprotein in plasma which is considered to modulate a coagulation and fibrinolysis system with the ability to bind to heparin, plasminogen, fibrinogen, thrombospondin, etc. Recently we have elucidated the primary structure of HRG by determining the nucleotide sequence of its cDNA, and showed that HRG is composed of several different types of internal repeats, each one of which shows considerable homology with the functional and/or structural domains of other proteins including high molecular weight kininogen, antithrombin III, cystatins, and proline-rich protein and peptide. Thus, the multifunctional property of HRG was suggested to be due to its multi-domain structure. In the present studies, a human genomic DNA library, cloned in the bacteriophage vector Charon 4A, was screened for HRG gene using a full-length cDNA coding for human IMI as a probe. A total of 7 clones were isolated from 6 × 105 phage and each was plaque purified. The entire HRG gene is represented in 3 genomic inserts with overlapping sequences that carry human DNA spanning 30 kb. Overlapping gene fragments were subcloned into pUC9 and characterized by Southern blot hybridization using 5’ and 3’ end probes isolated from human HRG cDNA and by DNA sequencing. These studies have shown that the gene for human HRG spans about 9 kb and consists of at least 5 exons and 4 introns. The putative histidine-rich region consisted of 12 tandemly repeated sequences of a 5 amino acid segment and 2 proline-rich regions contiguous to it are likely to be involved within one exon.

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Spiegler, V., M. Lubisch, A. Hensel, and E. Liebau. "The nematode strikes back – C. elegans' proline-rich response to treatment with oligomeric procyanidins." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608552.

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Goodwin, Andrew, Liang Zheng, Ling Lin, Ivan O. Rosas, and Danielle Morse. "Small Proline Rich Repeat Protein 1A Protects Against Epithelial Apoptosis And Is A Downstream Target Of WNT Proteins." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5997.

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Nair, Binoj C., Samaya R. Krishnan, Gangadhara R. Sareddy, Monica Mann, Bo Xu, Mohan Natarajan, Rajeshwar Rao Tekmal, and Ratna K. Vadlamudi. "Abstract 2135: Proline, glutamic acid, leucine rich protein 1 (PELP1) is essential for optimal p53-mediated DNA damage response." 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.am2012-2135.

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Sareddy, Gangadhara R., Pratibha Nutalapati, Rajeshwar R. Tekmal, and Ratna K. Vadlamudi. "Abstract 5190: The proto-oncogene Proline Glutamic acid Leucine rich Protein1 (PELP1) is a novel mediator of glioblastoma development." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5190.

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Hosono, Y., R. Nakashima, Y. Hajime, M. Kosaku, O. Koichiro, and T. Mimori. "366 Splicing factor proline/glutamine-rich (sfpq) is a novel autoantigen of anti-mda5 antibody-positive dermatomyositis/clinically amyopathic dermatomyositis." In LUPUS 2017 & ACA 2017, (12th International Congress on SLE &, 7th Asian Congress on Autoimmunity). Lupus Foundation of America, 2017. http://dx.doi.org/10.1136/lupus-2017-000215.366.

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Tassew, D., and Y. Tesfaigzi. "The Proline-Rich Domain of p53 Protects from Mucin Gene Expression at Baseline and After Short-Term but Not Chronic Wood Smoke Exposures." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a7330.

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Martin, Joshua A., Dana Gunderson, and Randall J. Kimple. "Abstract 4899: Small proline rich protein 3 (SPRR3) is a potential mediator of radiation resistance in HPV negative head and neck squamous cell carcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4899.

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Reports on the topic "Proline-rich"

1

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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Abstract:

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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