Characterization of four rice mutants with alterations in the defence response pathway
MOLECULAR PLANT PATHOLOGY
Authors: Campbell, MA; Ronald, PC
Abstract
A fast-neutron mutagenized population of rice seedlings was screened with Magnaporthe grisea, the causal agent of rice blast disease, to identify mutants with alterations in the defence response. Three mutant lines, ebr1, ebr2 and ebr3 (enhanced blast resistance) were identified that display enhanced resistance to M. grisea. ebr1 and ebr3 also confer enhanced resistance to the bacterial pathogen Xanthomonas oryzae pv. oryzae (Xoo). ebr3 develops a lesion mimic (LM) phenotype upon inoculation with M. grisea, and the phenotype is also induced by a shift in environmental conditions. The fourth mutant line, ncr1 (necrosis in rice), has an LM phenotype under all conditions tested and lacks enhanced resistance to either M. grisea or Xoo. Complementation testing using the mutant lines ebr3 and ncr1 indicates that the ebr3 and ncr1 loci are nonallelic and recessive. ebr1 and ebr2 display no alterations in expression of the rice pathogenesis-related (PR) genes PBZ1 and PR1, compared to wild-type C039. ebr3 has an elevated expression of PBZ1 and PR1 only in tissue displaying the LM phenotype. ncr1 strongly expresses PBZ1 in tissue displaying the LM phenotype, whereas PR1 expression in this tissue is similar to wild-type C039.
Genomic organization of the ILT11 gene, a novel member of the Leukocyte Receptor Cluster (LRC)
ACTIVATING AND INHIBITORY IMMUNOGLOBULIN-LIKE RECEPTORS
Authors: Wende, H; Ziegler, A; Volz, A
Abstract
The chromosomal region 19q13.4 harbors the human leukocyte receptor cluster (LRC) which has been demonstrated to contain over 25 genes encoding leukocyte-expressed receptors of the immunoglobulin superfamily. Among these are the killer cell inhibitory receptors (KIR), immunoglobulin like transcripts (ILT), leukocyte associated inhibitory receptors (LAIR), the Fc receptor for IgA (FCAR) as well as the gene for NCR1. ILTs are a family of homologous receptors with two or four immunoglobulin domains. We have determined the genomic organization of ILT11, a novel member of this family that comprises only two immunoglobulin domains. These are most homologous to the first and second immunoglobulin domain of four domain ILTs. ILT11 has a short cytoplasmic tail and a charged amino acid in its transmembrane region, which is characteristic of an activatory receptor. Additionally, the translation starts at a different codon, if compared to other family members.
COA
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