Molecular Biology and Evolution, Vol 12, 773-781, Copyright © 1995 by Society for Molecular Biology and Evolution
P Gonzalez, PV Rao, SB Nunez and JS Zigler Jr
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.
ORIGINAL ARTICLE
Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents
National Institutes of Health, Laboratory of Mechanisms of Ocular Diseases, National Eye Institute, Bethesda, Maryland 20892, USA.
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