Complexity of Hsp90 in organelle targeting

dc.contributor.author	Prassinos, C	en
dc.contributor.author	Haralampidis, K	en
dc.contributor.author	Milioni, D	en
dc.contributor.author	Samakovli, D	en
dc.contributor.author	Krambis, K	en
dc.contributor.author	Hatzopoulos, P	en
dc.date.accessioned	2014-06-06T06:48:24Z
dc.date.available	2014-06-06T06:48:24Z
dc.date.issued	2008	en
dc.identifier.issn	01674412	en
dc.identifier.uri	http://dx.doi.org/10.1007/s11103-008-9322-8	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/4126
dc.subject	Alternative transcription	en
dc.subject	Chloroplasts	en
dc.subject	Heat shock	en
dc.subject	Hsp90	en
dc.subject	Mitochondria	en
dc.subject	Targeting	en
dc.subject.other	heat shock protein 90	en
dc.subject.other	messenger RNA	en
dc.subject.other	primer DNA	en
dc.subject.other	alternative RNA splicing	en
dc.subject.other	amino acid sequence	en
dc.subject.other	Arabidopsis	en
dc.subject.other	article	en
dc.subject.other	cell organelle	en
dc.subject.other	chemistry	en
dc.subject.other	fluorescence microscopy	en
dc.subject.other	genetic transcription	en
dc.subject.other	genetics	en
dc.subject.other	metabolism	en
dc.subject.other	molecular genetics	en
dc.subject.other	nucleotide sequence	en
dc.subject.other	physiology	en
dc.subject.other	reverse transcription polymerase chain reaction	en
dc.subject.other	sequence homology	en
dc.subject.other	Alternative Splicing	en
dc.subject.other	Amino Acid Sequence	en
dc.subject.other	Arabidopsis	en
dc.subject.other	Base Sequence	en
dc.subject.other	DNA Primers	en
dc.subject.other	HSP90 Heat-Shock Proteins	en
dc.subject.other	Microscopy, Fluorescence	en
dc.subject.other	Molecular Sequence Data	en
dc.subject.other	Organelles	en
dc.subject.other	Reverse Transcriptase Polymerase Chain Reaction	en
dc.subject.other	RNA, Messenger	en
dc.subject.other	Sequence Homology, Amino Acid	en
dc.subject.other	Transcription, Genetic	en
dc.subject.other	Arabidopsis	en
dc.title	Complexity of Hsp90 in organelle targeting	en
heal.type	journalArticle	en
heal.identifier.primary	10.1007/s11103-008-9322-8	en
heal.publicationDate	2008	en
heal.abstract	Heat shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone. In Arabidopsis, the Hsp90 gene family consists of seven members. Here, we report that the AtHsp90-6 gene gives rise to two mRNA populations, termed AtHsp90-6L and AtHsp90-6S due to alternative initiation of transcription. The AtHsp90-6L and AtHsp90-6S transcription start sites are located 228 nucleotides upstream and 124 nucleotides downstream of the annotated translation start site, respectively. Both transcripts are detected under normal or heat-shock conditions. The inducibility of AtHsp90-6 mRNAs by heat shock implies a potential role of both isoforms in stress management. Stable transformation experiments with fusion constructs between the N-terminal part of each AtHsp90-6 isoform and green fluorescent protein indicated import of both fusion proteins into mitochondria. In planta investigation confirmed that fusion of the AtHsp90-5 N-terminus to green fluorescent protein (GFP) did result in specific chloroplastic localization. The mechanisms of regulation for mitochondria- and plastid-localized chaperone-encoding genes are not well understood. Future work is needed to address the possible roles of harsh environmental conditions and developmental processes on fine-tuning and compartmentalization of the AtHsp90-6L, AtHsp90-6S, and AtHsp90-5 proteins in Arabidopsis. © 2008 Springer Science+Business Media B.V.	en
heal.journalName	Plant Molecular Biology	en
dc.identifier.issue	4	en
dc.identifier.volume	67	en
dc.identifier.doi	10.1007/s11103-008-9322-8	en
dc.identifier.spage	323	en
dc.identifier.epage	334	en