ArticleJournal of molecular evolution1995
Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins.
Article in Journal of molecular evolution, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 65 citations in OpenAlex.
- Article
- Contributions of aquatic organisms to understanding the vertebrate ocular lens.Frontiers in ophthalmology · 2026Review
- Membrane structures and functional correlates in the bi-segmented eye lens of the cephalopod.Biology open · 2024Article
- Genome and transcriptome mechanisms driving cephalopod evolution.Nature communications · 2022Article
- Evolution and development of complex eyes: a celebration of diversity.Development (Cambridge, England) · 2020Review
- Global impact of diet and temperature over aquaculture of Octopus vulgaris paralarvae from a transcriptomic approach.Scientific reports · 2019Article
- Protein refractive index increment is determined by conformation as well as composition.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- Eye patches: Protein assembly of index-gradient squid lenses.Science (New York, N.Y.) · 2017Article
- Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive Protein.Scientific reports · 2016Article
- Molecular Evidence for Convergence and Parallelism in Evolution of Complex Brains of Cephalopod Molluscs: Insights from Visual Systems.Integrative and comparative biology · 2015Article
- Dead enzymes in the aldehyde dehydrogenase gene family: role in drug metabolism and toxicology.Expert opinion on drug metabolism & toxicology · 2015Review
- The molecular refractive function of lens γ-Crystallins.Journal of molecular biology · 2011Article
- Evolution of graded refractive index in squid lenses.Journal of the Royal Society, Interface · 2007Article
- Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Crystallin genes: specialization by changes in gene regulation may precede gene duplication.Journal of structural and functional genomics · 2003Review
- Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.The Biochemical journal · 2001Review
- J3-crystallin of the jellyfish lens: similarity to saposins.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Homology modeling of cephalopod lens S-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity.Biophysical journal · 1999Article
- Squid Pax-6 and eye development.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Enlightenment of old ideas from new investigations: more questions regarding the evolution of bacteriogenic light organs in squids.Evolution & developmentArticle
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Our previous studies have shown that the S-crystallins of cephalopod (Ommastrephes sloani pacificus) eye lenses comprise a family of at least ten members which are evolutionarily related to glutathione S-transferase (GST, EC 2.5.1.18). Here we show by cDNA cloning that there are at least 24 different S-crystallins that are 46-99% identical to each other by amino acid sequence in the squid Loligo opalescens. In each species, all but one S-crystallin (SL11 in O. pacificus and Lops4 in L. opalescens) examined has an inserted central peptide of variable length and sequence. cDNA expression studies conducted in Escherichia coli showed that squid GST (which is expressed little in the lens) has very high enzymatic activity using 1-chloro-2, 4-dinitrobenzene (CDNB) as a substrate; by contrast, SL20-1 of O. pacificus and Lops12 of L. opalescens (which are encoded by abundant lens mRNAs) have no GST activity. Interestingly, SL11 and Lops4 have some enzymatic activity with the CDNB substrate. Site-specific mutations at Y7 or W38, both residues essential for activity of vertebrate GSTs, or insertion of the central peptide present in the inactive SL20-1, reduced the specific activity of squid GST by 30- to 100-fold. These data indicate that the S-crystallins consist of a family of enzymatically inactive proteins (when using CDNB as a substrate) which is considerably larger than previously believed and that GST activity was lost by gradual drift in sequence as well as by insertion of an extra peptide by exon shuffling. The results are also consistent with the idea that SL11 and Lops4 are orthologous crystallins representing the first descendants of the ancestral GST gene in the pathway which gave rise to the extensive S-crystallin family of lens proteins.
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