Differential regulation of a hydroxyproline-rich glycoprotein gene family in wounded and infected plants

We have characterized three different transcripts induced by fungal elicitor, wounding, or infection which encode apoproteins of cell wall hydroxyproline-rich glycoproteins involved in plant defense against infection. The proteins encoded by two of these transcripts contain a proline-rich domain involving tandem repetition of the 16-amino-acid unit Tyr3-Lys-Ser-Pro4-Ser-Pro-Ser-Pro4. The third transcript encodes a protein with a proline-rich domain involving a variant of this 16-mer canonical repeat: Tyr3-His-Ser-Pro4-Lys-His-Ser-Pro4. Each transcript is encoded by a separate gene present at single or low copy number in the haploid genome. These transcripts exhibit markedly different patterns of accumulation in different stress conditions, indicating the operation of several distinct intercellular stress signal systems in higher plants.

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Structural characterization of the third scavenger receptor cysteine‐rich domain of murine neurotrypsin

Protein Science ◽

10.1002/pro.3587 ◽

2019 ◽

Vol 28 (4) ◽

pp. 746-755 ◽

Cited By ~ 5

Author(s):

Anselmo Canciani ◽

Gianluca Catucci ◽

Federico Forneris

Keyword(s):

Structural Characterization ◽

Scavenger Receptor ◽

The Third ◽

Rich Domain ◽

Cysteine Rich Domain

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Cyclic guanosine monophosphate as a mediator in processes of stress-signal transduction in higher plants

BIOPHYSICS ◽

10.1134/s0006350915040089 ◽

2015 ◽

Vol 60 (4) ◽

pp. 559-570 ◽

Cited By ~ 1

Author(s):

L. V. Dubovskaya ◽

Y. S. Bakakina ◽

I. D. Volotovski

Keyword(s):

Signal Transduction ◽

Higher Plants ◽

Cyclic Guanosine Monophosphate ◽

Guanosine Monophosphate ◽

Stress Signal

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Differential regulation of CXCR4 and CCR5 endocytosis

Journal of Cell Science ◽

10.1242/jcs.111.18.2819 ◽

1998 ◽

Vol 111 (18) ◽

pp. 2819-2830 ◽

Cited By ~ 1

Author(s):

N. Signoret ◽

M.M. Rosenkilde ◽

P.J. Klasse ◽

T.W. Schwartz ◽

M.H. Malim ◽

...

Keyword(s):

Phorbol Ester ◽

Chemokine Receptors ◽

Phorbol Esters ◽

Virus Entry ◽

Cell Receptor ◽

Differential Regulation ◽

Significant Component ◽

Cellular Activation ◽

Rich Domain ◽

Stromal Cell Derived Factor

The chemokine receptors CCR5 and CXCR4 are major co-receptors/receptors for the CD4-dependent and CD4-independent entry of human and simian immunodeficiency viruses. The chemokines that bind and activate these receptors can inhibit the entry of viruses that use the respective co-receptor molecules. Chemokine-induced co-receptor internalisation is a significant component of the mechanism through which chemokines inhibit virus entry. CXCR4 internalisation is induced by the CXCR4 ligand stromal cell derived factor-1 (SDF-1), phorbol esters and, in T cells, cellular activation. Here we show that CXCR4 endocytosis can be mediated through either one of two distinct internalisation signals. A COOH-terminal serine rich domain is required for ligand- but not phorbol ester- induced CXCR4 internalisation. However, a Ser/IleLeu motif, similar to that required for the endocytosis of CD4 and the T cell receptor/CD3 complex, is required for phorbol ester-induced, but not ligand-induced, CXCR4 endocytosis. By contrast, CCR5 internalisation is induced by the beta-chemokine RANTES but not by phorbol esters. CCR5 lacks the Ser/IleLeu sequence required for phorbol ester-induced uptake of CXCR4. Together these results indicate that distinct mechanisms can regulate CXCR4 and CCR5 endocytosis and trafficking.

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Two distinct domains of Bicoid mediate its transcriptional downregulation by the Torso pathway

Development ◽

10.1242/dev.128.12.2281 ◽

2001 ◽

Vol 128 (12) ◽

pp. 2281-2290

Author(s):

Florence Janody ◽

Rachel Sturny ◽

Valérie Schaeffer ◽

Yannick Azou ◽

Nathalie Dostatni

Keyword(s):

Transcriptional Activity ◽

Drosophila Embryo ◽

Anterior Pole ◽

Activation Domain ◽

Activation Domains ◽

The Third ◽

Signal Transduction Cascade ◽

Rich Domain ◽

Global Activity

The transcriptional activity of the Bicoid morphogen is directly downregulated by the Torso signal transduction cascade at the anterior pole of the Drosophila embryo. This regulation does not involve the homeodomain or direct phosphorylation of Bicoid. We analyse the transcriptional regulation of Bicoid in response to the Torso pathway, using Bicoid variants and fusion proteins between the Bicoid domains and the Gal4 DNA-binding domain. We show that Bicoid possesses three autonomous activation domains. Two of these domains, the serine/threonine-rich and the acidic domains, are downregulated by Torso, whereas the third activation domain, which is rich in glutamine, is not. The alanine-rich domain, previously described as an activation domain in vitro, has a repressive activity that is independent of Torso. Thus, Bicoid downregulation by Torso results from a competition between the glutamine-rich domain that is insensitive to Torso and the serine/threonine-rich and acidic activation domains downregulated by Torso. The alanine-rich domain contributes to this process indirectly by reducing the global activity of the protein and in particular the activity of the glutamine-rich domain that might otherwise prevent downregulation by Torso.

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Effect of foliar urea application on quality, growth, mineral uptake and yield of broccoli (Brassica oleracea L., var. italica)

Plant Soil and Environment ◽

10.17221/2227-pse ◽

2008 ◽

Vol 53 (No. 3) ◽

pp. 120-128 ◽

Cited By ~ 18

Author(s):

E. Yildirim ◽

I. Guvenc ◽

M. Turan ◽

A. Karatas

Keyword(s):

Dry Matter ◽

Mineral Content ◽

Higher Plants ◽

Nutrient Content ◽

Growth And Yield ◽

Nitrogen Application ◽

Mineral Uptake ◽

The Third ◽

Almost All ◽

Foliar Urea

The objective of this study was to determine the effect of foliar urea applications on quality, growth, mineral content and yield of broccoli under field conditions in 2003, 2004 and 2005. Broccoli cultivars AG 3317 and AG 3324 were treated with foliar urea applications at different concentrations (0.0, 0.4, 0.8 and 1.0%). Foliar applications of urea, especially 0.8 and 1.0% resulted in larger heads, weightier heads and plants as well as higher plants. Conversely, the greatest head and leaf dry matter contents were obtained with no fertilizer-nitrogen application. SPAD chlorophyll readings that were measured in the third year increased with elevated urea concentrations. In regard to the nutrient content, it can be interfered that soil nitrogen fertilization and foliar urea applications increased the content of almost all nutrients in leaves and heads of both broccoli cultivars in three experiment years. Generally, the greatest values were obtained from 1.0% urea application for both cultivars. It results from the study that for optimum yields 0.61 and 0.96% concentrations of urea sprays could be successfully used to obtain better growth and yield in broccoli cultivars AG 3317 and AG 3324, respectively.

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Crystal Structure of the Cysteine-Rich Domain of Mannose Receptor Complexed with a Sulfated Carbohydrate Ligand

Journal of Experimental Medicine ◽

10.1084/jem.191.7.1105 ◽

2000 ◽

Vol 191 (7) ◽

pp. 1105-1116 ◽

Cited By ~ 83

Author(s):

Yang Liu ◽

Arthur J. Chirino ◽

Ziva Misulovin ◽

Christine Leteux ◽

Ten Feizi ◽

...

Keyword(s):

Mannose Receptor ◽

Pituitary Hormones ◽

Carbohydrate Binding ◽

Fibroblast Growth ◽

The Third ◽

Rich Domain ◽

Sulfated Carbohydrate ◽

Carbohydrate Ligand ◽

Macrophage Uptake ◽

Cysteine Rich Domain

The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of infectious organisms, and the NH2-terminal cysteine-rich domain (Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To elucidate the mechanism of sulfated carbohydrate recognition, we determined crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 Å resolution, respectively. Cys-MR folds into an approximately three-fold symmetric β-trefoil shape resembling fibroblast growth factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native crystals bind in a neutral pocket in the third lobe. We use the structures to rationalize the carbohydrate binding specificities of Cys-MR and compare the recognition properties of Cys-MR with other β-trefoil proteins.

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Gene Cloning, Characterization, and Molecular Simulations of a Novel Recombinant Chitinase from Chitinibacter Tainanensis CT01 Appropriate for Chitin Enzymatic Hydrolysis

Polymers ◽

10.3390/polym12081648 ◽

2020 ◽

Vol 12 (8) ◽

pp. 1648

Author(s):

Yeng-Tseng Wang ◽

Po-Long Wu

Keyword(s):

Enzymatic Hydrolysis ◽

Hydrogen Bonds ◽

Gene Cloning ◽

Genome Sequence ◽

Higher Plants ◽

Molecular Simulations ◽

Experimental Results ◽

Glycosidic Linkage ◽

The Third ◽

Recombinant Chitinase

Chitin, a polymer of N-acetyl-d-glucosamine (GlcNAc), can be degraded by chitinase, which is produced by higher plants, vertebrates, and bacteria. Chitinases are characterized by the ability to hydrolyze the beta-1,4-linkages in the chitin chain by either an endolytic or an exolytic mechanism. Chitinase 1198 is a novel endochitinase from the genome sequence of Chitinibacter tainanensis CT01. Herein, we report the findings of molecular simulations and bioassays for chitinase 1198. Our experimental results suggest that chitinase 1198 can recognize the nonreducing end of chitin and cleave the second or third glycosidic linkage from the nonreducing end of chitin oligomers. Furthermore, our simulations results revealed that chitinase 1198 is more likely to bind chitin oligomers with the main hydrogen bonds of the Asp440, the second GlcNAc unit of chitin oligomers, and degrade chitin oligomers to (GlcNAc)2 molecules. Moreover, chitinase 1198 is less likely to bind chitin oligomers with the main hydrogen bonds of the Asp440, the third GlcNAc unit of chitin oligomers, and degrade chitin oligomers to (GlcNAc)3 molecules. Lastly, chitinase 1198 can bind (GlcNAc)3 molecules with the main hydrogen bonds of the Asp440, the second GlcNAc of the (GlcNAc)3 molecules, and degrade chitin oligomers to GlcNAc and (GlcNAc)2 molecules.

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