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J. Biol. Chem., Vol. 275, Issue 52, 41064-41073, December 29, 2000
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From the While many of the diverse crystallins of the
transparent lens of vertebrates are related or identical to metabolic
enzymes, much less is known about the lens crystallins of
invertebrates. Here we investigate the complex eye of scallops.
Electron microscopic inspection revealed that the anterior, single
layered corneal epithelium overlying the cellular lens contains a
regular array of microvilli that we propose might contribute to its
optical properties. The sole crystallin of the scallop eye lens was
found to be homologous to The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF148508.
-Crystallin of the Scallop Lens
A DIMERIC ALDEHYDE DEHYDROGENASE CLASS 1/2
ENZYME-CRYSTALLIN*
§,
,,,, and§§
Laboratory of Molecular and Developmental
Biology and ** Laboratory of Mechanisms of Ocular Disease, National Eye
Institute, and Center for Molecular
Modeling, Center for Information Technology, National Institutes of
Health, Bethesda, Maryland 20892, the ¶ Laboratory of
Transcriptional Regulation, Institute of Molecular Genetics, Prague 6, Czech Republic, and the Jules Stein Eye Institute, UCLA
School of Medicine, Los Angeles, California 90095
-crystallin, a minor crystallin in
cephalopods related to aldehyde dehydrogenase (ALDH) class 1/2. Scallop
-crystallin (officially designated ALDH1A9) is 55-56% identical to
its cephalopod homologues, while it is 67 and 64% identical to human
ALDH 2 and 1, respectively, and 61% identical to retinaldehyde
dehydrogenase/
-crystallin of elephant shrews. Like other
enzyme-crystallins, scallop -crystallin appears to be present in low
amounts in non-ocular tissues. Within the scallop eye,
immunofluorescence tests indicated that -crystallin expression is
confined to the lens and cornea. Although it has conserved the critical
residues required for activity in other ALDHs and appears by homology
modeling to have a structure very similar to human ALDH2, scallop
-crystallin was enzymatically inactive with diverse substrates and
did not bind NAD or NADP. In contrast to mammalian ALDH1 and -2 and
other cephalopod -crystallins, which are tetrameric proteins,
scallop -crystallin is a dimeric protein. Thus, ALDH is the most
diverse lens enzyme-crystallin identified so far, having been used as a
lens crystallin in at least two classes of molluscs as well as elephant shrews.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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