Crystallins of the octopus lens. Recruitment from detoxification enzymes.
The eye lens crystallins of the octopus Octopus dofleini were identified by sequencing abundant proteins and cDNAs. As in squid, the octopus crystallins have subunit molecular masses of 25-30 kDa, are related to mammalian glutathione S-transferases (GST), and are encoded in at least six genes. The coding regions and deduced amino acid sequences of four octopus lens cDNAs are 75-80% identical, while their non-coding regions are entirely different. Deduced amino acid sequences show 52-57% similarity with squid GST-like crystallins, but only 20-25% similarity with mammalian GST. These data suggest that the octopus and squid lens GST-like crystallin gene families expanded after divergence of these species. Northern blot hybridization indicated that the four octopus GST-like crystallin genes examined are lens-specific. Lens extracts showed about 40 times less GST activity using 1-chloro-2,4-dinitrobenzene as substrate than liver extracts of the octopus, indicating that the major GST-like crystallins are specialized for a lens structural role. A prominent 59-kDa crystallin polypeptide, previously observed in octopus but not squid and called omega-crystallin (Chiou, S.-H. (1988) FEBS Lett. 241, 261-264), has been identified as an aldehyde dehydrogenase. Since cytoplasmic aldehyde dehydrogenase is a major protein in elephant shrew lenses (eta-crystallin; Wistow, G., and Kim, H. (1991) J. Mol. Evol. 32, 262-269) the octopus aldehyde dehydrogenase crystallin provides the first example of a similar enzyme-crystallin in vertebrates and invertebrates. The use of detoxification stress proteins (GST and aldehyde dehydrogenase) as cephalopod crystallins indicates a common strategy for recruitment of enzyme-crystallins during the convergent evolution of vertebrate and invertebrate lenses. For historical reasons we propose that the octopus GST-like crystallins, like those of the squid, are called S-crystallins.
Tomarev
S I
SI
Laboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892.
Zinovieva
R D
RD
Piatigorsky
J
J
D000444:Aldehyde Dehydrogenase / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D015152:Blotting, Northern; D003001:Cloning, Molecular; D003459:Crystallins / Q000235:genetics* / Q000302:isolation & purification; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D049832:Decapodiformes / Q000235:genetics; D015723:Gene Library; D005982:Glutathione Transferase / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000235:genetics*; D007908:Lens, Crystalline / Q000502:physiology*; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D005810:Multigene Family; D049831:Octopodiformes / Q000235:genetics*; D009838:Oligodeoxyribonucleotides; D012313:RNA / Q000235:genetics / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D003459:Crystallins; D007527:Isoenzymes; D009838:Oligodeoxyribonucleotides; D012313:RNA; D004247:DNA; D000444:Aldehyde Dehydrogenase; D005982:Glutathione Transferase