120- and 160-kDa Receptors for Endogenous Mitogenic Peptide, Phytosulfokine-α, in Rice Plasma Membranes

Matsubayashi, Yoshikatsu; Sakagami, Youji

doi:10.1074/jbc.275.20.15520

Cited by 68 publications

(25 citation statements)

References 34 publications

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“…The binding of a defense polypeptide signal in plants raised the question of whether plants may use other polypeptide hormones to regulate defensive or developmental processes. Since 1991, several other polypeptide signals have been reported in plants that include two 18-aa glycosylated systemins from tobacco (2), phytosulfokines (13), small sulfated 4-to 5-aa polypeptides that regulate cell proliferation and differentiation (14), CLAVATA3 (15), a 73-aa polypeptide from Arabidopsis meristems with a role in development (16), and 55-to 58-aa cystine-rich polypeptides (SCRs) that regulate selfincompatibility in Brassica (17,18).…”

Section: Resultsmentioning

confidence: 99%

RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development

Pearce

Moura

Stratmann

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

398

442

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A 5-kDa polypeptide was isolated from tobacco leaves that induced a rapid alkalinization of the culture medium of tobacco suspension-cultured cells and a concomitant activation of an intracellular mitogen-activated protein kinase. An N-terminal sequence was obtained, and a cDNA coding for the 49-aa polypeptide was isolated from a tobacco cDNA library. The cDNA encoded a preproprotein of 115 amino acids that contained the polypeptide at its C terminus. A search among known expressed sequence tags revealed that genes encoding Rapid ALkalinization Factor (RALF) preproproteins were present in various tissues and organs from 16 species of plants representing 9 families. A tomato homolog of the polypeptide was synthesized and, when supplied to germinating tomato and Arabidopsis seeds, it caused an arrest of root growth and development. Although its specific role in growth has not been established, the polypeptide joins the ranks of the increasing number of polypeptide hormones that are known to regulate plant stress, growth, and development

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Section: Resultsmentioning

confidence: 99%

RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development

Pearce

Moura

Stratmann

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

398

442

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“…To test the specificity of the photoaffinity labeling, the IRBCs were first incubated with underivatized C4S oligosaccharide, the nonradiolabeled photoactive derivative (40 g), or heparin (20 g) at 37°C for 30 min (43). The IRBCs were washed with PBS, pH 7.2, and then labeled with 125 I-labeled N-4-azidosalicylyl derivative of C4S dodecasaccharide as described above.…”

Section: Methodsmentioning

confidence: 99%

“…The N-deacetylated C4S dodecasaccharide (200 g) was dissolved in 200 l of PBS, pH 7.2, and 75 g of NHS-ASA in Me 2 SO (20 l) was added (43,44). After stirring overnight at room temperature in the dark, solid NaHCO 3 was added to saturation, and then 10 l of 10% acetic anhydride in acetone was added two times at 10-min intervals to N-acetylate the remainder of the -NH 2 groups.…”

Section: Methodsmentioning

confidence: 99%

“…Radioiodination of the Photoactivable Probe-Na 125 I solution (10 l, 1 mCi) and two Iodobeads were added to a solution of N-4-azidosalicylyl derivative of C4S dodecasaccharide (40 g) in 100 l of PBS, pH 7.2 (42,43). The solution was allowed to stand at room temperature for 1 h in the dark and then chromatographed on Sephadex G-15 columns (0.6 ϫ 30 cm) using 0.2 M NaCl.…”

Section: Methodsmentioning

confidence: 99%

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Structural Basis for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin 4-Sulfate and Design of Novel Photoactivable Reagents for the Identification of Parasite Adhesive Proteins

Gowda¹,

Madhunapantula²,

Achur

et al. 2007

Journal of Biological Chemistry

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A dodecasaccharide motif of the low-sulfated chondroitin 4-sulfate (C4S) mediate the binding of Plasmodium falciparuminfected red blood cells (IRBCs) in human placenta. Here we studied the detailed C4S structural requirements by assessing the ability of chemically modified C4S to inhibit IRBC binding to the placental chondroitin sulfate proteoglycan. Replacement of the N-acetyl groups with bulky N-acyl or N-benzoyl substituents had no effect on the inhibitory activity of C4S, whereas reduction of the carboxyl groups abrogated the activity. Dermatan sulfates showed ϳ50% inhibitory activity when compared with C4Ss with similar sulfate contents. These data demonstrate that the C4S carboxyl groups and their equatorial orientation but not the N-acetyl groups are critical for IRBC binding. Conjugation of bulky substituents to the reducing end N-acetylgalactosamine residues of C4S dodecasaccharide had no effect on its inhibitory activity. Based on these results, we prepared photoaffinity reagents for the identification of the parasite proteins involved in C4S binding. Cross-linking of the IRBCs with a radioiodinated photoactivable C4S dodecasaccharide labeled a ϳ22-kDa novel parasite protein, suggesting strongly for the first time that a low molecular weight IRBC surface protein rather than a 200 -400-kDa PfEMP1 is involved in C4S binding. Conjugation of biotin to the C4S dodecasaccharide photoaffinity probe afforded a strategy for the isolation of the labeled protein by avidin affinity precipitation, facilitating efforts to identify the C4S-adherent IRBC protein(s). Our results also have broader implications for designing oligosaccharide-based photoaffinity probes for the identification of proteins involved in glycosaminoglycan-dependent attachment of microbes to hosts.An unusual feature of Plasmodium falciparum infection compared with the three other human malarial parasites, Plasmodium vivax, Plasmodium ovale, and Plasmodium malariae, is that only the former parasite is able to sequester in the microvascular capillaries of various organs (1, 2). In P. falciparuminfected individuals, the infected red blood cells (IRBCs) 5 adhere to the vascular endothelial surface by binding to the cell adhesion molecules. This adherence property is believed to play an important role in the development of cerebral and other severe malaria syndromes (2-4). Several host molecules have been implicated in the IRBC adherence, including thrombospondin, CD36, intercellular adhesion molecule 1, vascular cell adhesion molecule 1, E-selectin, P-selectin, platelet endothelial cell adhesion molecule/CD31, and chondroitin 4-sulfate (1-6). In response to the development of adherent phenotypespecific immunity by hosts, parasites with different adherent receptor specificity evolve to efficiently survive in the host. However, eventually, when immunity to various adhesive parasite phenotypes is developed, the host effectively controls infection and avoids pathogenesis. This is generally true for malaria-immune people regardless of gender. However, in ...

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“…As with animal polypeptides hormones, plant polypeptide signals act as extracellular ligands that are functionally perceived by high-affinity plasma-membrane-bound receptors (9)(10)(11)(12)(13)(14). Systemin, an 18-aa polypeptide, was identified in 1991 as the primary signal for the systemic activation of defense genes in leaves of wounded tomato plants (1).…”

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confidence: 99%

The systemin receptor SR160 from Lycopersicon peruvianum is a member of the LRR receptor kinase family

Scheer

Ryan

2002

Proc. Natl. Acad. Sci. U.S.A.

286

128

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The isolation to homogeneity of the 160-kDa systemin cell-surface receptor (SR160) from plasma membranes of suspension cultured cells of Lycopersicon peruvianum is reported. The purification procedure resulted in recovery of 13 g of pure receptor protein, representing an 8,200-fold purification. Gel blot analyses using SR160-specific antibodies confirmed that a cross-reacting protein in the membranes of suspension-cultured cells comigrates with both the native and a deglycosylated form of the radiolabeled receptor. Internal amino acid sequences of the purified protein facilitated the isolation of a cDNA clone encoding the 160-kDa receptor. The identity of the encoded protein as SR160 was further confirmed by a comparison of its sequence with a mass spectral fingerprint of the SR160 protein. The deduced amino acid sequence of SR160 revealed that it is a member of the leucine-rich repeat (LRR) receptor kinase family, closely related to the brassinolide receptor kinase, BRI1.tomato ͉ jasmonic acid ͉ systemic wound signaling ͉ brassinolide receptor P olypeptide hormones have recently been identified in plants as key regulatory signals for defense, reproduction, growth, and development (1-8). As with animal polypeptides hormones, plant polypeptide signals act as extracellular ligands that are functionally perceived by high-affinity plasma-membrane-bound receptors (9-14). Systemin, an 18-aa polypeptide, was identified in 1991 as the primary signal for the systemic activation of defense genes in leaves of wounded tomato plants (1). Systemin causes a cascade of intracellular signaling events leading to the release of linolenic acid from membranes, and its conversion to oxylipin molecules that signal defense gene expression (15)(16)(17)(18)(19)(20). These events are initiated by the release of systemin at wound sites and its interaction with a membrane-bound receptor (9,10,21). A photoaffinity analog of systemin was used to identify a 160-kDa cell-surface receptor protein in membranes of Lycopersicon peruvianum suspension cultured cells that possessed characteristics of a systemin receptor (10). We report here that the radioactive photoaffinity label provided a marker for purification of the receptor protein to homogeneity. Amino acid sequence analysis allowed the cloning of the receptor cDNA from a L. peruvianum cDNA library and the identification of the cDNA-encoded protein as a leucine-rich repeat (LRR) receptor kinase with high amino acid identity and domain similarities to the BRI1 receptor kinase from Arabidopsis. Materials and MethodsCell Culture. Suspension cultures of L. peruvianum were grown in media under conditions previously described (10). One-liter cultures were grown in 4-liter Fernbach flasks initially inoculated with 50 ml of 1-week-old cells grown in 125-ml Erlenmeyer flasks. The cells were grown for 1 week under the same growth conditions and media reported (10).125 I-azido-Cys-3,Ala-15-systemin. N-[4-(p-azidosalicylamido) butyl]-3Ј[2Ј-Cys-3,Ala-15-systemindithiol] propionamide, or azidoCys-3,Ala-15-...

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120- and 160-kDa Receptors for Endogenous Mitogenic Peptide, Phytosulfokine-α, in Rice Plasma Membranes

Cited by 68 publications

References 34 publications

RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development

RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development

Structural Basis for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin 4-Sulfate and Design of Novel Photoactivable Reagents for the Identification of Parasite Adhesive Proteins

The systemin receptor SR160 from Lycopersicon peruvianum is a member of the LRR receptor kinase family

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