Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods.

Tomarev, S.I.; Zinovieva, R. D.; Guo, Kai; Piatigorsky, Joram

doi:10.1016/s0021-9258(18)53643-7

Cited by 89 publications

(19 citation statements)

References 53 publications

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“…After assembly, we found 53 unique S-crystallin transcripts. The predicted protein sequences are very similar to known S-crystallin sequences, with 52.0 ± 15.0% amino acid identity and 60.9 ± 12.9% similarity to Lops8, an archived S-crystallin from Loligo opalescens chosen for comparison (GenBank U19296.1) (18). In the 53 unique S-crystallins in the transcriptome, we identified 43 unique loop sequences that varied in length from 3 to 110 amino acids (Fig.…”

Section: Rna Sequencingmentioning

confidence: 71%

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Eye patches: Protein assembly of index-gradient squid lenses

Cai

Townsend

Dodson

et al. 2017

Science

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A parabolic relationship between lens radius and refractive index allows spherical lenses to avoid spherical aberration. We show that in squid, patchy colloidal physics resulted from an evolutionary radiation of globular S-crystallin proteins. Small angle x-ray scattering experiments on lens tissue show colloidal gels of S-crystallins at all radial positions. Sparse lens materials form via low-valence linkages between disordered loops protruding from the surface. The arms are polydisperse and bind via a set of hydrogen bonds between disordered side chains. Peripheral lens regions with low particle valence form stable, volume-spanning gels at low density, while central regions with higher average valence gel at higher densities. The proteins demonstrate an evolved set of linkers for self-assembly of nanoparticles into volumetric materials.

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Section: Rna Sequencingmentioning

confidence: 71%

“…Given the age of extant S-crystallin studies and subsequent improvements in sequencing technologies, it was important to ensure that we had captured the full range of S-crystallin genetic diversity expressed in the squid lens (17)(18)(19). Therefore, we sequenced transcriptomes of mature lens tissue from Doryteuthis pealeii.…”

Section: Rna Sequencingmentioning

confidence: 99%

Eye patches: Protein assembly of index-gradient squid lenses

Cai

Townsend

Dodson

et al. 2017

Science

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“…However, it is enough to substantially affect the substrate specificity of a given isoenzyme. In this regard, it is interesting to note that GSH transferases such as the a class isoenzymes (Mannervik et al, 1985) or the squid enzyme (Tomarev et al, 1993), which do not have a tyrosine residue at the equivalent position of Y115, are not particularly good for catalyzing epoxide ring openings or Michael additions.3 The structural and functional evidence suggests that Y115 acts as a general-acid catalytic group.…”

Section: Discussionmentioning

confidence: 99%

Structure and Function of the Xenobiotic Substrate Binding Site of a Glutathione S-Transferase as Revealed by X-ray Crystallographic Analysis of Product Complexes with the Diastereomers of 9-(S-Glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene

Ji¹,

Johnson²,

Sesay³

et al. 1994

Biochemistry

119

100

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The three-dimensional structures of isoenzyme 3-3 of glutathione (GSH) transferase complexed with (9R,10R)- and (9S,10S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene [(9R,10R)-2 and (9S,10S)-2], which are the products of the addition of GSH to phenanthrene 9,10-oxide, have been determined at resolutions of 1.9 and 1.8 A, respectively. The structures indicate that the xenobiotic substrate binding site is a hydrophobic cavity defined by the side chains of Y6, W7, V9, and L12 from domain I (the GSH binding domain) and I111, Y115, F208, and S209 in domain II of the protein. All of these residues are located in variable-sequence regions of the primary structure of class mu isoenzymes. Three of the eight residues (V9, I111, and S209) of isoenzyme 3-3 that are in direct van der Waals contact with the dihydrophenanthrenyl portion of the products are mutated (V9I, I111A, and S209A) in the related isoenzyme 4-4. These three residues are implicated in control of the stereoselectivity of the class mu isoenzymes. The hydroxyl group of Y115 is found to be hydrogen-bonded to the 10-hydroxyl group of (9S,10S)-2, a fact suggesting that this residue could act as an electrophile to stabilize the transition state for the addition of GSH to epoxides. The Y115F mutant isoenzyme 3-3 is about 100-fold less efficient than the native enzyme in catalyzing the addition of GSH to phenanthrene 9,10-oxide and about 50-fold less efficient in the Michael addition of GSH to 4-phenyl-3-buten-2-one. The side chain of Y115 is positioned so as to act as a general-acid catalytic group for two types of reactions that would benefit from electrophilic assistance. The results are consistent with the notion that domain II, which harbors most of the variability in primary structure, plays a crucial role in defining the substrate specificity of class mu isoenzymes.

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“…It may therefore play a role in the secretion itself, as part of the defense mechanism, or the mechanism of secretion itself. While the gene duplication of GST has been identified as the source of enzymatically inactive crystallins in the development of cephalopod lens refraction, 49 at least one active GST enzyme has been identified in the digestive gland of squids. 49 When compared against Swiss-Prot and BLAST databases, the protein was more closely aligned with other aquatic snails, such as Reishia clavigera and Cipangopaludina cathayensis, than any known squid lens protein.…”

Section: ■ Discussionmentioning

confidence: 99%

Comparative Proteomic Analysis of Slime from the Striped Pyjama Squid, Sepioloidea lineolata, and the Southern Bottletail Squid, Sepiadarium austrinum (Cephalopoda: Sepiadariidae)

et al. 2019

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Sepioloidea lineolata, the striped pyjama squid (family Sepiadariidae), is a small species of benthic bobtail squid distributed along the Southern Indo-Pacific coast of Australia. Like other sepiadariid squids, it is known to secrete large volumes of viscous slime when stressed. In order to identify key proteins involved in the function of sepiadariid slimes, we compared the slime proteome of Sepioloidea lineolata with that of a closely related species, Sepiadarium austrinum. Of the 550 protein groups identified in Sepioloidea lineolata slime, 321 had orthologs in Sepiadarium austrinum, and the abundance of these (iBAQ) was highly correlated between species. Both slimes were dominated by a small number of abundant proteins, and several of these were short secreted proteins with no homologues outside the class Cephalopoda. No mucins were identified within either species' slime, suggesting that it is structurally distinct from mucin polymer-based gels found in many vertebrate and echinoderm secretions. The extent of N-glycosylation in the slime of Sepioloidea lineolata was also studied via glycan cleavage with Peptide: N-glycosidase F (PNGase-F). Although very few (four) proteins showed strong evidence of Nglycosylation, we found that treatment with PNGase-F led to a slight increase in peptide identification rates compared with controls.

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Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods.

Cited by 89 publications

References 53 publications

Eye patches: Protein assembly of index-gradient squid lenses

Eye patches: Protein assembly of index-gradient squid lenses

Structure and Function of the Xenobiotic Substrate Binding Site of a Glutathione S-Transferase as Revealed by X-ray Crystallographic Analysis of Product Complexes with the Diastereomers of 9-(S-Glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene

Comparative Proteomic Analysis of Slime from the Striped Pyjama Squid, Sepioloidea lineolata, and the Southern Bottletail Squid, Sepiadarium austrinum (Cephalopoda: Sepiadariidae)

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