Sequence of a Glycine-Rich Protein from Lizard Claw: Unusual Dilute Acid and Heptafluorobutyric Acid Cleavages

Inglis, A.S.; Gillespie, J. M.; Roxburgh, C. M.; Whittaker, Lois A.; Casagranda, Franca

doi:10.1007/978-1-4613-1787-6_77

Cited by 32 publications

(53 citation statements)

References 9 publications

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“…The alignment of the other sequences is one of several alternative possibilities. That shown maximizes the alignment of proline residues and is similar to the one used in our earlier studies a O'Donnell (1973) b O'Donnell and Inglis (1974) c Presland et al (1989): the same sequences is present in duck (Anas platyrhynchos) and pigeon (Columba livia)- Arai et al (1986) d Sawyer et al (2003) e Walker and Bridgen (1976) f Inglis et al (1987) g Whitbread et al (1991) h Toni et al (2007a) i Toni et al (2007b) j Dalla β-sheets in mammalian keratin…”

Section: An Additional β-Sheet In Lizard Clawsupporting

confidence: 71%

The role of β-sheets in the structure and assembly of keratins

Fraser

2009

Biophys Rev

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X-ray diffraction, infrared and electron microscope studies of avian and reptilian keratins, and of stretched wool and hair, have played a central role in the development of models for the β-conformation in proteins. Both α-and β-keratins contain sequences that are predicted to adopt a β-conformation and these are believed to play an important part in the assembly of the filaments and in determining their mechanical properties. Interactions between the small β-sheets in keratins provide a simple mechanism through which shape and chemical complementarity can mediate the assembly of molecules into highly specific structures. Interacting β-sheets in crystalline proteins are often related to one another by diad symmetry and the data available on feather keratin suggest that the filament is assembled from dimers in which the β-sheets are related by a perpendicular diad. The most detailed model currently available is for feather and reptilian keratin but the presence of related β-structural forms in mammalian keratins is also noted.

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Section: An Additional β-Sheet In Lizard Clawsupporting

confidence: 71%

The role of β-sheets in the structure and assembly of keratins

Fraser

2009

Biophys Rev

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“…12). Gecko sequences resemble that of the lizard P. sicula (Dalla Valle et al, 2005) but are very different from that of a hard keratin protein isolated from the claw of the varanus lizard (Inglis et al, 1987). Gecko ␤-keratins are a little larger (1-2 kDa) than ␤-keratins of P. sicula, and this finding may be a specialization of tuberculate scales of geckoes.…”

Section: Discussionmentioning

confidence: 96%

“…Generally, ␤-keratins have a smaller molecular weight (10 -22 kDa) than ␣-(soft)-keratins (40 -68 kDa; Brush, 1979, 1983;Sawyer et al, 2000;Alibardi and Toni, 2006a,b). The number of ␤-keratins in reptilian epidermis, their amino acid sequences, and spatial conformation are only known for a lizard claw (Inglis et al, 1987), and for a scale keratin (Dalla Valle et al, 2005) to date. The latter study showed the expression of ␤-keratin mRNAs in both oberhautchen and ␤-cells of lizard epidermis.…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of scale β‐keratins in the differentiating epidermis of geckoes show they are glycine‐proline‐serine–rich proteins with a central motif homologous to avian β‐keratins

Valle

Nardi

Toffolo

et al. 2006

Developmental Dynamics

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“…Some studies on claw keratins have demonstrated that high-sulfur beta-keratins occur in the claw (Inglis et al 1987) while low sulfur betakeratins prevail in ordinary scales (Dalla Valle et al 2005, 2007a, 2007b. Present histochemical findings are consistent with occurrence of sulfydryl groups and suggest that numerous disulfuric bonds are formed in the mature corneous material, resulting in the improvement of the mechanical properties of claws.…”

Section: Process Of Hard Cornificationmentioning

confidence: 99%

Cornification in developing claws of the common Australian skink (Lampropholis guichenoti) (Squamata, Lacertidae)

Alibardi

2008

Italian Journal of Zoology

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An ultrastructural and immunocytochemical study on developing lizard claws has been done. Claws originate from an epidermal thickening covering the tip of digits under which mesenchymal cells aggregate. The outer side of the dorsal terminal scale of a digit gives origin to the unguis, and suggests that claws are modified scales sustained by the last phalanx. Beneath four-seven layers of embryonic alpha-keratin cells, beta-keratin cells are differentiated but no shedding complex is formed. Beta-keratin cells extends also over the apical part of the ventral side (sub-unguis) which is mainly formed by alphakeratin cells. Initially beta-keratin filaments have a prevalent oblique orientation along the plane containing the proximalapical axis of the digit. Later bundles become more irregularly distributed. Beta-keratin cells of the unguis remain largely separated and do not merge into a syncitium like in the beta-layer of scales. The thickness of the horny layer is higher in the unguis than in the sub-unguis and decreases from the claw tip toward its basal most part. It is hypothesized that the evolution of claws occurred by the extension of the outer scale surface of the terminal scales beyond the digit tip under the influence of the apical mesenchyme in the terminal phalange.

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Sequence of a Glycine-Rich Protein from Lizard Claw: Unusual Dilute Acid and Heptafluorobutyric Acid Cleavages

Cited by 32 publications

References 9 publications

The role of β-sheets in the structure and assembly of keratins

The role of β-sheets in the structure and assembly of keratins

Cloning and characterization of scale β‐keratins in the differentiating epidermis of geckoes show they are glycine‐proline‐serine–rich proteins with a central motif homologous to avian β‐keratins

Cornification in developing claws of the common Australian skink (Lampropholis guichenoti) (Squamata, Lacertidae)

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