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- Autor Nach Häufigkeit alphabetisch sortiert
- Abel, S. (1)
- Asquini, E. (1)
- De Nardi, B. (1)
- Del Terra, L. (1)
- Dreos, R. (1)
- Gasperini, D. (1)
- Graziosi, G. (1)
- Levy, M. (1)
- Martellossi, C. (1)
- Pacchioni, B. (1)
- Pallavicini, A. (1)
- Rathinavelu, R. (1)
- Savchenko, T. (1)
- Tornincasa, P. (1)
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De Nardi, B.; Dreos, R.; Del Terra, L.; Martellossi, C.; Asquini, E.; Tornincasa, P.; Gasperini, D.; Pacchioni, B.; Rathinavelu, R.; Pallavicini, A.; Graziosi, G. Differential responses of Coffea arabica L. leaves and roots to chemically induced systemic acquired resistance Genome 49, 1594-1605, (2006) DOI: 10.1139/g06-125
Coffea arabica is susceptible to several pests
and diseases, some of which affect the leaves and roots. Systemic
acquired resistance (SAR) is the main defence mechanism activated in
plants in response to pathogen attack. Here, we report the effects of
benzo(1,2,3)thiadiazole-7-carbothioic acid-s-methyl ester (BTH), a SAR
chemical inducer, on the expression profile of C. arabica. Two cDNA
libraries were constructed from the mRNA isolated from leaves and
embryonic roots to create 1587 nonredundant expressed sequence tags
(ESTs). We developed a cDNA microarray containing 1506 ESTs from the
leaves and embryonic roots, and 48 NBS-LRR (nucleotide-binding site
leucine-rich repeat) gene fragments derived from 2 specific genomic
libraries. Competitive hybridization between untreated and BTH-treated
leaves resulted in 55 genes that were significantly overexpressed and 16
genes that were significantly underexpressed. In the roots, 37 and 42
genes were over and underexpressed, respectively. A general shift in
metabolism from housekeeping to defence occurred in the leaves and roots
after BTH treatment. We observed a systemic increase in
pathogenesis-related protein synthesis, in the oxidative burst, and in
the cell wall strengthening processes. Moreover, responses in the roots
and leaves varied significantly.
Abel, S.; Savchenko, T.; Levy, M. Genome-wide comparative analysis of the <em>IQD</em> gene families in <em>Arabidopsis thaliana</em> and Oryza sativa BMC Evolutionary Biology 5, 72 (1-25), (2005)
We identified and analyzed 33 and 29 IQD1-like genes in Arabidopsis thaliana and Oryza sativa, respectively. The encoded IQD proteins contain a plant-specific domain of 67 conserved amino acid residues, referred to as the IQ67 domain, which is characterized by a unique and repetitive arrangement of three different calmodulin recruitment motifs, known as the IQ, 1-5-10, and 1-8-14 motifs. We demonstrated calmodulin binding for IQD20, the smallest IQD protein in Arabidopsis, which consists of a C-terminal IQ67 domain and a short N-terminal extension. A striking feature of IQD proteins is the high isoelectric point (~10.3) and frequency of serine residues (~11%). We compared the Arabidopsis and rice IQD gene families in terms of gene structure, chromosome location, predicted protein properties and motifs, phylogenetic relationships, and evolutionary history. The existence of an IQD-like gene in bryophytes suggests that IQD proteins are an ancient family of calmodulin-binding proteins and arose during the early evolution of land plants. Comparative phylogenetic analyses indicate that the major IQD gene lineages originated before the monocot-eudicot divergence. The extant IQD loci in Arabidopsis primarily resulted from segmental duplication and reflect preferential retention of paralogous genes, which is characteristic for proteins with regulatory functions. Interaction of IQD1 and IQD20 with calmodulin and the presence of predicted calmodulin binding sites in all IQD family members suggest that IQD proteins are a new class of calmodulin targets. The basic isoelectric point of IQD proteins and their frequently predicted nuclear localization suggest that IQD proteins link calcium signaling pathways to the regulation of gene expression. Our comparative genomics analysis of IQD genes and encoded proteins in two model plant species provides the first step towards the functional dissection of this emerging family of putative calmodulin targets.