zeta-Crystallin is a protein highly expressed in the lens of guinea pi
gs and camels, where it comprises about 10% of the total soluble prote
in. It has recently been characterized as a novel quinone oxidoreducta
se present in a variety of mammalian tissues. We report here the isola
tion and characterization of the human zeta-crystallin gene (CRYZ) and
its processed pseudogene. The functional gene is composed of nine exo
ns and spans about 20 kb. The 5'-flanking region of the gene is rich i
n G and C (58%) and lacks TATA and CAAT boxes. Previous analysis of th
e guinea pig gene revealed the presence of two different promoters, on
e responsible for the high lens-specific expression and the other for
expression at the enzymatic level in numerous tissues. Comparative ana
lysis with the guinea pig gene shows that a region of similar to 2.5 k
b that includes the promoter responsible for the high expression in th
e lens in guinea pig is not present in the human gene. (C) 1994 Academ
ic Press, Inc.