Evidence for independent recruitment of ζ-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents

P. Gonzalez, P. V. Rao, S. B. Nunez, J. S. Zigler

Research output: Contribution to journalArticlepeer-review

Abstract

Zeta-crystallin/quinone reductase (CRYZ) is an NADPH oxidoreductase expressed at very high levels in the lenses of two groups of mammals: camelids and some hystricomorph rodents. It is also expressed at very low levels in all other species tested. Comparative analysis of the mechanisms mediating the high expression of this enzyme/crystallin in the lens of the llama (Lama guanacoe) and the guinea pig (Cavia porcellus) provided evidence for independent recruitment of this enzyme as a lens crystallin in both species and allowed us to elucidate for the first time the mechanism of lens recruitment of an enzyme-crystallin. The data presented here show that in both species such recruitment most likely occurred through the generation of new lens promoters from nonfunctional intron sequences by the accumulation of point mutations and/or small deletions and insertions. These results further support the idea that recruitment of CRYZ resulted from an adaptive process in which the high expression of CRYZ in the lens provides some selective advantage rather than from a purely neutral evolutionary process.

Original languageEnglish (US)
Pages (from-to)773-781
Number of pages9
JournalMolecular biology and evolution
Volume12
Issue number5
StatePublished - Jan 1 1995

Keywords

  • enzyme/crystallin
  • guinea pig
  • llama
  • ocular lens
  • promoter evolution
  • promoter function
  • recruitment of crystallins

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Genetics

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