Keratin intermediate filament chains in tuatara (Sphenodon punctatus): A comparison of tuatara and human sequences
•The sequences of 25 Type I and Type II keratin intermediate filament chains from tuatara are reported.•The head and tail sequences in human and tuatara show significant differences.•The KAPs in human trichocyte α-keratins do not have direct equivalents in tuatara. Determination of the sequences of...
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Published in | Journal of structural biology Vol. 213; no. 1; p. 107706 |
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Format | Journal Article |
Language | English |
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01.03.2021
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Abstract | •The sequences of 25 Type I and Type II keratin intermediate filament chains from tuatara are reported.•The head and tail sequences in human and tuatara show significant differences.•The KAPs in human trichocyte α-keratins do not have direct equivalents in tuatara.
Determination of the sequences of the keratin intermediate filament chains in tuatara has shown that these are closely akin to the α-keratins in human and other vertebrates, especially in the central, coiled-coil rod region. The domain lengths within the rod are preserved exactly, both Type I and Type II chains have been recognised, and sequence identity/homology exists between their respective chains. Nonetheless, there are characteristic differences in amino acid composition and sequence between their respective head (N-terminal) domains and their tail (C-terminal) domains, though some similarities are retained. Further, there is evidence of tandem repeats of a variety of lengths in the tuatara heads and tails indicative of sequence duplication events. These are not evident in human α-keratins and would therefore have implications for the physical attributes of the tissues in the two species. Multiple families of keratin-associated proteins that are ultra-high cysteine-rich or glycine + tyrosine-rich in human and other species do not have direct equivalents in the tuatara. Although high-sulphur proteins are present in tuatara the cysteine residue contents are significantly lower than in human. Further, no sequence homologies between the HS proteins in the two species have been found, thereby casting considerable doubt as to whether any matrix-forming high-sulphur proteins exist in tuatara. These observations may be correlated with the numerous cysteine-rich β-keratins (corneous β-proteins) that are present in tuatara, but which are conspicuously absent in mammals. |
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AbstractList | Determination of the sequences of the keratin intermediate filament chains in tuatara has shown that these are closely akin to the α-keratins in human and other vertebrates, especially in the central, coiled-coil rod region. The domain lengths within the rod are preserved exactly, both Type I and Type II chains have been recognised, and sequence identity/homology exists between their respective chains. Nonetheless, there are characteristic differences in amino acid composition and sequence between their respective head (N-terminal) domains and their tail (C-terminal) domains, though some similarities are retained. Further, there is evidence of tandem repeats of a variety of lengths in the tuatara heads and tails indicative of sequence duplication events. These are not evident in human α-keratins and would therefore have implications for the physical attributes of the tissues in the two species. Multiple families of keratin-associated proteins that are ultra-high cysteine-rich or glycine + tyrosine-rich in human and other species do not have direct equivalents in the tuatara. Although high-sulphur proteins are present in tuatara the cysteine residue contents are significantly lower than in human. Further, no sequence homologies between the HS proteins in the two species have been found, thereby casting considerable doubt as to whether any matrix-forming high-sulphur proteins exist in tuatara. These observations may be correlated with the numerous cysteine-rich β-keratins (corneous β-proteins) that are present in tuatara, but which are conspicuously absent in mammals. •The sequences of 25 Type I and Type II keratin intermediate filament chains from tuatara are reported.•The head and tail sequences in human and tuatara show significant differences.•The KAPs in human trichocyte α-keratins do not have direct equivalents in tuatara. Determination of the sequences of the keratin intermediate filament chains in tuatara has shown that these are closely akin to the α-keratins in human and other vertebrates, especially in the central, coiled-coil rod region. The domain lengths within the rod are preserved exactly, both Type I and Type II chains have been recognised, and sequence identity/homology exists between their respective chains. Nonetheless, there are characteristic differences in amino acid composition and sequence between their respective head (N-terminal) domains and their tail (C-terminal) domains, though some similarities are retained. Further, there is evidence of tandem repeats of a variety of lengths in the tuatara heads and tails indicative of sequence duplication events. These are not evident in human α-keratins and would therefore have implications for the physical attributes of the tissues in the two species. Multiple families of keratin-associated proteins that are ultra-high cysteine-rich or glycine + tyrosine-rich in human and other species do not have direct equivalents in the tuatara. Although high-sulphur proteins are present in tuatara the cysteine residue contents are significantly lower than in human. Further, no sequence homologies between the HS proteins in the two species have been found, thereby casting considerable doubt as to whether any matrix-forming high-sulphur proteins exist in tuatara. These observations may be correlated with the numerous cysteine-rich β-keratins (corneous β-proteins) that are present in tuatara, but which are conspicuously absent in mammals. |
ArticleNumber | 107706 |
Author | Parry, David A.D. Winter, David J. |
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CitedBy_id | crossref_primary_10_1007_s00709_023_01865_3 crossref_primary_10_1186_s12862_023_02107_z crossref_primary_10_1016_j_cbd_2023_101116 crossref_primary_10_1016_j_jsb_2021_107793 crossref_primary_10_3390_genes12040591 |
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Keywords | Epidermal appendages UHS Mya HGT EDC Reptilian keratin Mechanical properties KIF KAP HS Intermediate filament chains Sequence repeats |
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Snippet | •The sequences of 25 Type I and Type II keratin intermediate filament chains from tuatara are reported.•The head and tail sequences in human and tuatara show... Determination of the sequences of the keratin intermediate filament chains in tuatara has shown that these are closely akin to the α-keratins in human and... |
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SubjectTerms | Epidermal appendages Intermediate filament chains Mechanical properties Reptilian keratin Sequence repeats |
Title | Keratin intermediate filament chains in tuatara (Sphenodon punctatus): A comparison of tuatara and human sequences |
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