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Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2AThe heterotrimeric protein phosphatase 2A (PP2A) is a component of multiple signaling pathways in eukaryotes. Disruption of PP2A activity in Arabidopsis is known to alter auxin transport and growth response pathways. We demonstrated that the regulatory subunit A of an Arabidopsis PP2A interacts with a novel cyclophilin, ROC7. The gene for this cyclophilin encodes a protein that contains a unique 30-amino acid extension at the N-terminus, which distinguishes the gene product from all previously identified Arabidopsis cyclophilins. Altered forms of ROC7 cyclophilin with mutations in the conserved DENFKL domain did not bind to PP2A. Unlike protein phosphatase 2B, PP2A activity in Arabidopsis extracts was not affected by the presence of the cyclophilin-binding molecule cyclosporin. The ROC7 transcript was expressed to high levels in all tissues tested. Expression of an ROC7 antisense transcript gave rise to increased root growth. These results indicate that cyclophilin may have a role in regulating PP2A activity, by a mechanism that differs from that employed for cyclophilin regulation of PP2B.
Document ID
20040141715
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Jackson, K.
(Yale University New Haven, CT 06520-8114, United States)
Soll, D.
Evans, M. L.
Date Acquired
August 22, 2013
Publication Date
December 1, 1999
Publication Information
Publication: Molecular & general genetics : MGG
Volume: 262
Issue: 5-Apr
ISSN: 0026-8925
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: GM51101
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Plant Biology
Non-NASA Center

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