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http://purl.uniprot.org/citations/22476462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22476462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22476462http://www.w3.org/2000/01/rdf-schema#comment"The homeodomain transcription factor KNOTTED1 (KN1) functions in shoot meristem maintenance and is thought to move from cell to cell in a similar fashion as viral movement proteins. Both types of transported proteins bind to RNA, and associate with intercellular bridges formed by plasmodesmata. In a mutant screen for KN1 transport deficiency, a component of a type II chaperonin complex, CCT8, was identified, and found to interact with non-cell-autonomous proteins. The cct8 mutants are characterized by limited functionality of non-cell-autonomous proteins after their movement, and a phenotype resembling lack of homeodomain protein activity. Evidence suggests that CCT8 functions in post-translocational refolding of transported proteins. Here we show that spread of tobamovirus infection is reduced in a cct8 mutant. This suggests that similar to KN1, viral movement proteins are unfolded and refolded during transport to gain functionality in the receiving cells."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.org/dc/terms/identifier"doi:10.4161/psb.19152"xsd:string
http://purl.uniprot.org/citations/22476462http://purl.org/dc/terms/identifier"doi:10.4161/psb.19152"xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Jackson D."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Jackson D."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Kragler F."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Kragler F."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Xu X.M."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Xu X.M."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Fichtenbauer D."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/author"Fichtenbauer D."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/name"Plant Signal. Behav."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/name"Plant Signal. Behav."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/pages"318-321"xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/pages"318-321"xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/title"The chaperonin CCT8 facilitates spread of tobamovirus infection."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/title"The chaperonin CCT8 facilitates spread of tobamovirus infection."xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/22476462http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/22476462http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22476462
http://purl.uniprot.org/citations/22476462http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22476462