The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein

Nature. 1989 Mar 2;338(6210):67-70. doi: 10.1038/338067a0.


Mutations of the Drosophila melanogaster ninaA gene affect phototransduction: ninaA mutant flies have a 10-fold reduction in the levels of rhodopsin in the R1-R6 photoreceptor cells. The ninaA gene was isolated and found to encode a 237-amino-acid protein that has over 40% amino-acid sequence identity with the vertebrate cyclosporin A-binding protein, cyclophilin, a protein that seems to be involved in T-lymphocyte activation. The remarkable evolutionary conservation of cyclophilin in two phylogenetically distant organisms and its involvement in diverse transduction processes suggests that this protein plays an important role in cellular metabolism. Indeed, cyclophilin has recently been shown to be a prolyl cis-trans isomerase that catalyses, in vitro, rate-limiting steps in the folding of a number of proteins. Here, we present evidence for the involvement of cyclophilin-like molecules in a defined cellular process. The availability of mutations in a cyclophilin gene provides a new model system for the study of cyclophilin and cyclosporin action.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins / genetics*
  • Cloning, Molecular
  • Cyclosporins / metabolism
  • Drosophila melanogaster / genetics*
  • Drosophila melanogaster / physiology
  • Genes*
  • Molecular Sequence Data
  • Mutation
  • Peptidylprolyl Isomerase
  • Photoreceptor Cells / physiology
  • Restriction Mapping
  • Retinal Pigments / genetics*
  • Rhodopsin / genetics*
  • Rhodopsin / physiology
  • Sequence Homology, Nucleic Acid
  • Vision, Ocular*


  • Carrier Proteins
  • Cyclosporins
  • Retinal Pigments
  • Rhodopsin
  • Peptidylprolyl Isomerase