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Amino acid sequence of the carboxy‐terminal part of an acidic type I cytokeratin of molecular weight 51 000 from Xenopus laevis epidermis as predicted from the cDNA sequence.
Author(s) -
Hoffmann W.,
Franz J.K.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01966.x
Subject(s) - xenopus , biology , microbiology and biotechnology , complementary dna , cytokeratin , epidermis (zoology) , peptide sequence , cdna library , keratin , amino acid , keratin 6a , biochemistry , cytoskeleton , gene , genetics , intermediate filament , anatomy , cell , immunohistochemistry , immunology
The DNA sequence of a clone from a cDNA library made from Xenopus laevis skin is described. This sequence represents the 3′‐terminal end of an mRNA which codes for an epidermal cytokeratin polypeptide of mol. wt. 51 000 of the acidic (type I) subfamily as identified by hybridization‐selection of mRNAs, followed by gel electrophoretic identification of the polypeptides synthesized by translation in vitro. The partial amino acid sequence of the amphibian cytokeratin shows strong similarity to type I cytoskeletal keratins from human (mol. wt. 50 000) and murine (mol. wt. 59 000) epidermis. In the non alpha‐helical tail region the human and the non‐mammalian (Xenopus) keratins are more similar to each other than to the murine protein, indicating that the former are equivalent cytokeratin polypeptides and belonging to a special subclass of type I keratin polypeptides devoid of glycine‐rich regions in the carboxy‐terminal portion. The evolutionary conservativity of the genes coding for cytokeratins is discussed.