Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA

Brian Ondek; Robert W Hardy; Elizabeth K Baker; Mark A Stamnes; Bih-Hwa Shieh; Charles S Zuker

doi:10.1016/S0021-9258(18)42025-X

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Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA

Journal article

Open access

Peer reviewed

Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA

Brian Ondek, Robert W Hardy, Elizabeth K Baker, Mark A Stamnes, Bih-Hwa Shieh and Charles S Zuker

The Journal of biological chemistry, Vol.267(23), pp.16460-16466

01/01/1992

DOI: 10.1016/S0021-9258(18)42025-X

PMID: 1644830

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Abstract

Cyclophilins, the intracellular receptors for the widely used immunosuppressant cyclosporin A have been found to be peptidyl-prolyl cis/trans isomerases and have been implicated in intracellular protein folding and trafficking. The Drosophila ninaA gene encodes a photoreceptor-specific cyclophilin homolog involved in rhodopsin biogenesis. ninaA mutants have a 90% reduction in the levels of Rh1 rhodopsin. We carried out a genetic screen designed to identify functionally important regions in the ninaA protein. Over 700,000 mutagenized flies were screened for a visible ninaA phenotype and 70 independent mutations in ninaA were isolated and characterized. These mutations provide a detailed dissection of the structure/function relationships in cyclophilin. We also show that mammalian cyclophilins engineered to contain missense mutations found in two temperature-sensitive ninaA alleles display temperature-sensitive prolyl cis/trans isomerase activity.

cyclophilin

Drosophila

site-directed mutagenesis

structure-activity relationships

Details

Title: Subtitle: Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA
Creators: Brian Ondek - University of California San Diego
Robert W Hardy - University of California San Diego
Elizabeth K Baker - University of California San Diego
Mark A Stamnes - University of California San Diego
Bih-Hwa Shieh - University of California San Diego
Charles S Zuker - University of California San Diego
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.267(23), pp.16460-16466
DOI: 10.1016/S0021-9258(18)42025-X
PMID: 1644830
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Language: English
Date published: 01/01/1992
Academic Unit: Molecular Physiology and Biophysics; Internal Medicine
Record Identifier: 9984297605002771

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