| http://purl.uniprot.org/citations/18467340 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18467340 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18467340 | http://www.w3.org/2000/01/rdf-schema#comment | "PYK10/BGLU23 is a beta-glucosidase that is a major protein of ER bodies, which are endoplasmic reticulum (ER)-derived organelles that may be involved in defense systems. PYK10 has active and inactive forms. Active PYK10 molecules form large complexes with diameters ranging from 0.65 microm to > 70 microm. We identified three beta-glucosidases (PYK10, BGLU21 and BGLU22), five jacalin-related lectins (JALs) and a GDSL lipase-like protein (GLL) in the purified PYK10 complex. Expression levels of JALs and GLLs were lower in the nai1-1 mutant, which has no ER bodies, than in Col-0. The subcellular localization of PYK10 is predicted to be different from the localizations of JALs and GLLs. This suggests that PYK10 interacts with its partners (JALs and GLLs) when the subcellular structure is destroyed by pathogens. The PYK10 complex was found to be larger in the pbp1-1 and jal22-1 mutants than in Col-0, while it was smaller in the jal23-1, jal31-1 and jal31-2 mutants than in Col-0. These results show that two types of JALs having opposite roles regulate the size of the PYK10 complex antagonistically. We define the two types of lectins as a 'polymerizer-type lectin' and an 'inhibitor-type lectin'. Interestingly, the closest homologs of polymerizer-type lectins (JAL31 and JAL23) were inhibitor-type lectins (PBP1/JAL30 and JAL22). The pairs of polymerizer-type and inhibitor-type lectins reported here are good examples of genes that have evolved new functions after gene duplication (neofunctionalization)."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.org/dc/terms/identifier | "doi:10.1093/pcp/pcn075"xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.org/dc/terms/identifier | "doi:10.1093/pcp/pcn075"xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Fukao Y."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Fukao Y."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Hara-Nishimura I."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Hara-Nishimura I."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Nishimura M."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Nishimura M."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Fujiwara M."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Fujiwara M."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Nagano A.J."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/author | "Nagano A.J."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/name | "Plant Cell Physiol."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/name | "Plant Cell Physiol."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/pages | "969-980"xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/pages | "969-980"xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/title | "Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/title | "Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/volume | "49"xsd:string |
| http://purl.uniprot.org/citations/18467340 | http://purl.uniprot.org/core/volume | "49"xsd:string |