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

• Published in: Molecular biology and evolution 1995-09, Vol.12 (5), p.773-781
• Main Authors: Gonzalez, P, Rao, P V, Nuñez, S B, Zigler, Jr, J S
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological Evolution; Camelids, New World - genetics; Camelus - genetics; Cloning, Molecular; Crystallins - biosynthesis; Crystallins - genetics; DNA Primers; DNA, Complementary; Guinea Pigs - genetics; Humans; Lens, Crystalline - metabolism; Molecular Sequence Data; NAD(P)H Dehydrogenase (Quinone) - biosynthesis; NAD(P)H Dehydrogenase (Quinone) - genetics; Polymerase Chain Reaction; Rats - genetics; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid
• ISSN: 0737-4038; 1537-1719; 1537-1719
• DOI: 10.1093/oxfordjournals.molbev.a040255

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 Ilama (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.