Abstract:
:Protein phosphatase 2A (PP2A) is a serine/threonine-specific phosphatase comprising a catalytic subunit (C), a scaffolding subunit (A), and a regulatory subunit (B). The B subunits are believed to be responsible for substrate specificity and localization of the PP2A complex. In plants, three families of B subunits exist, i.e. B (B55), B', and B''. Here, we report differential subcellular targeting within the Arabidopsis B'eta subfamily, which consists of the close homologs B'eta, B'theta, B'gamma and B'zeta. Phenotypes of corresponding knockouts were observed, and particularly revealed delayed flowering for the B'eta knockout. The B' subunits were linked to fluorescent tags and transiently expressed in various tissues of onion, tobacco and Arabidopsis. B'eta and B'gamma targeted the cytosol and nucleus. B'zeta localized to the cytoplasm and partly co-localized with mitochondrial markers when the N-terminus was free. Provided its C-terminus was free, the B'theta subunit targeted peroxisomes. The importance of the C-terminal end for peroxisomal targeting was further confirmed by truncation of the C-terminus. The results revealed that the closely related B' subunits are targeting different organelles in plants, and exemplify the usage of the peptide serine-serine-leucine as a PTS1 peroxisomal signaling peptide.
journal_name
Plantajournal_title
Plantaauthors
Matre P,Meyer C,Lillo Cdoi
10.1007/s00425-009-0998-zsubject
Has Abstractpub_date
2009-10-01 00:00:00pages
935-45issue
5eissn
0032-0935issn
1432-2048journal_volume
230pub_type
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