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Molecular and Cellular Biology, October 2002, p. 6993-7003, Vol. 22, No. 20
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.20.6993-7003.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Cyclophilin A Peptidyl-Prolyl Isomerase Activity Promotes Zpr1 Nuclear Export

Husam Ansari,1 Giampaolo Greco,1 and Jeremy Luban1,2*

Departments of Microbiology,1 Medicine, Columbia University College of Physicians and Surgeons, New York, New York 100322

Received 29 April 2002/ Returned for modification 3 July 2002/ Accepted 10 July 2002

The peptidyl-prolyl isomerase (PPIase) cyclophilin A (Cpr1p) is conserved from eubacteria to mammals, yet its biological function has resisted elucidation. Unable to identify a phenotype that is suggestive of Cpr1p's function in a cpr1{Delta} Saccharomyces cerevisiae strain, we screened for CPR1-dependent strains. In all cases, dependence was conferred by mutations in ZPR1, a gene encoding an essential zinc finger protein. CPR1 dependence was suppressed by overexpression of EF1{alpha} (a translation factor that binds Zpr1p), Cpr6p (another cyclophilin), or Fpr1p (a structurally unrelated PPIase). Suppression by a panel of cyclophilin A mutants correlated with PPIase activity, confirming the relevance of this activity in CPR1-dependent strains. In CPR1+ cells, wild-type Zpr1p was distributed equally between the nucleus and cytoplasm. In contrast, proteins encoded by CPR1-dependent alleles of ZPR1 accumulated in the nucleus, as did wild-type Zpr1p in cpr1{Delta} cells. Transport kinetic studies indicated that nuclear export of Zpr1p was defective in cpr1{Delta} cells, and rescue of this defect correlated with PPIase activity. Our results demonstrate a functional interaction between Cpr1p, Zpr1p, and EF1{alpha}, a role for Cpr1p in Zpr1p nuclear export, and a biological function for Cpr1p PPIase activity.

* Corresponding author. Mailing address: Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 W. 168th St., HHSC 1502, New York, NY 10032. Phone: (212) 305-8706. Fax: (212) 305-0333. E-mail: JL45{at}columbia.edu.

Molecular and Cellular Biology, October 2002, p. 6993-7003, Vol. 22, No. 20
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.20.6993-7003.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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