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91.
A Nitrilase-Like Protein Interacts with GCC Box
DNA-Binding
Proteins Involved in Ethylene and
Defense Responses 总被引:5,自引:1,他引:4 下载免费PDF全文
Ping Xu Meena L. Narasimhan Teresa Samson Maria A. Coca Gyung-Hye Huh Jianmin Zhou Gregory B. Martin Paul M. Hasegawa Ray A. Bressan 《Plant physiology》1998,118(3):867-874
Ethylene-responsive element-binding proteins (EREBPs) of tobacco (Nicotiana tabacum L.) bind to the GCC box of many pathogenesis-related (PR) gene promoters, including osmotin (PR-5). The two GCC boxes on the osmotin promoter are known to be required, but not sufficient, for maximal ethylene responsiveness. EREBPs participate in the signal transduction pathway leading from exogenous ethylene application and pathogen infection to PR gene induction. In this study EREBP3 was used as bait in a yeast two-hybrid interaction trap with a tobacco cDNA library as prey to isolate signal transduction pathway intermediates that interact with EREBPs. One of the strongest interactors was found to encode a nitrilase-like protein (NLP). Nitrilase is an enzyme involved in auxin biosynthesis. NLP interacted with other EREBP family members, namely tobacco EREBP2 and tomato (Lycopersicon esculentum L.) Pti4/5/6. The EREBP2-EREBP3 interaction with NLP required part of the DNA-binding domain. The specificity of interaction was further confirmed by protein-binding studies in solution. We propose that the EREBP-NLP interaction serves to regulate PR gene expression by sequestration of EREBPs in the cytoplasm. 相似文献
92.
V Narasimhan D Holowka B Baird 《Biochemical and biophysical research communications》1990,171(1):222-229
Disruption of microfilaments in rat basophilic leukemia (RBL) cells by exposure to cytochalasin B is observed to potentiate the rate of antigen-stimulated secretion from these cells. Under these conditions, cytochalasin B is without effect on the antigen-stimulated production of inositol phosphates or 45Ca2(+)-influx. In streptolysin-O-permeabilized RBL cells, cytochalasin B is observed to potentiate the rate of secretion in response both to guanosine 5'-(2-thio)-O-triphosphate (GTP gamma S) and to Ca2+ (buffered between 0.1 and 10 microM). However, under these conditions, cytochalasin B does not affect to antigen-stimulated production of inositol phosphates. Consistent with these data, microfilaments are proposed to regulate a terminal step in exocytosis, in a physiologically relevant manner. 相似文献
93.
Kohrt JT Filipski KJ Cody WL Cai C Dudley DA Van Huis CA Willardsen JA Rapundalo ST Saiya-Cork K Leadley RJ Narasimhan L Zhang E Whitlow M Adler M McLean K Chou YL McKnight C Arnaiz DO Shaw KJ Light DR Edmunds JJ 《Bioorganic & medicinal chemistry letters》2005,15(21):4752-4756
The activated Factor VII/tissue factor complex (FVIIa/TF) plays a key role in the formation of blood clots. Inhibition of this complex may lead to new antithrombotic drugs. An X-ray crystal structure of a fluoropyridine-based FVIIa/TF inhibitor bound in the active site of the enzyme complex suggested that incorporation of substitution at the 5-position of the hydroxybenzoic acid side chain could lead to the formation of more potent inhibitors through interactions with the S1'/S2' pocket. 相似文献
94.
A natural shift is taking place in the approaches being adopted by plant scientists in response to the accessibility of systems-based
technology platforms. Metabolomics is one such field, which involves a comprehensive non-biased analysis of metabolites in
a given cell at a specific time. This review briefly introduces the emerging field and a range of analytical techniques that
are most useful in metabolomics when combined with computational approaches in data analyses. Using cases from Arabidopsis and other selected plant systems, this review highlights how information can be integrated from metabolomics and other functional
genomics platforms to obtain a global picture of plant cellular responses. We discuss how metabolomics is enabling large-scale
and parallel interrogation of cell states under different stages of development and defined environmental conditions to uncover
novel interactions among various pathways. Finally, we discuss selected applications of metabolomics.
This special review article is dedicated to the commemoration of the retirement of Dr. Oluf L. Gamborg after 25 years of service
as Founding Managing Editor of Plant Cell Reports. RB and KN have contributed equally to this review. 相似文献
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T. R. Narasimhan H. L. Kim S. H. Safe 《Journal of biochemical and molecular toxicology》1991,6(3):229-236
The effects of three tetrachlorobiphenylols [2′,3′,4′,5′-tetrachloro-2-biphenylol (1); 2′,3′,4′,5′-tetrachloro-4-biphenylol (2); and 2′,3′,4′,5′-tetrachloro-3-biphenylol (3)]; three monochlorobiphenylols [5-chloro-2-biphenylol (5), 3-chloro-2-biphenylol (6); and 2-chloro-4-biphenylol (7)] and a tetrachlorobiphenyldiol [3,3′,5,5′-tetrachloro-4,4′-biphenyldiol (4) on respiration, adenosine triphosphatase (ATPase)] activity, and swelling in isolated mouse liver mitochondria have been investigated. Tetrachlorobiphenylols (1–3) and the tetrachlorobiphenyldiol (4) inhibited state-3 respiration in a concentration-dependent manner with succinate as substrate (flavin adenine dinucleotide [FAD]-linked) and the tetrachlorobiphenyldiol (4) caused a more pronounced inhibitory effect on state-3 respiration than the other congeners. The monochlorobiphenylols 5–7 were less active as inhibitors of state-3 mitochondrial respiration and significant effects were observed only at higher concentration (≥0.4 μM). However, in the presence of the nicotinamide adenine dinucleotide (NAD)-linked substrates (glutamate plus malate), hydroxylated PCBs (1–7) significantly inhibited mitochondrial state-3 respiration in a concentration-dependent manner. Compounds 5, 6, and 7 uncoupled mitochondrial oxidative phosphorylation only in the presence of FAD-linked substrate as evidenced by increased oxygen consumption during state-4 respiratory transition, stimulating ATPase activity, releasing oligomycin-inhibited respiration, and inducing mitochondrial swelling (5, 6, and 7). Tetrachlorobiphenylols 1, 2, and 3 had no effect on mitochondrial ATPase activity while the tetrachlorobiphenyldiol, 4, decreased the enzyme activity. The possible inhibitory site of electron transport by these compounds and their toxicologic significance is discussed. 相似文献
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