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Publication : Complete sequence of the mouse type-II keratin EndoA: its amino-terminal region resembles mitochondrial signal peptides.

First Author  Ouellet T Year  1988
Journal  Gene Volume  70
Issue  1 Pages  75-84
PubMed ID  2467842 Mgi Jnum  J:9697
Mgi Id  MGI:58154 Doi  10.1016/0378-1119(88)90106-0
Citation  Ouellet T, et al. (1988) Complete sequence of the mouse type-II keratin EndoA: its amino-terminal region resembles mitochondrial signal peptides. Gene 70(1):75-84
abstractText  We have isolated a clone, pKA56, from a cDNA library prepared from poly(A)/RNA of F9ACc19 cells. Northern-blot analysis showed that this clone recognizes a 1.9-kb mRNA which is expressed strongly in F9 differentiated cells but only faintly detected in F9 stem cells. Sequence determination revealed that this mRNA codes for EndoA, the murine homologue of the human type-II keratin No. 8. This is the first report of the complete coding sequence of a mammalian keratin No. 8. Comparison of mouse EndoA with keratin No. 8 of humans, cows and frogs indicated a strong evolutionary conservation. The first 16 amino acid residues of the N-terminal domain of EndoA are also homologous to other type-II keratins and, to a lesser extent, to other intermediate filament (IF) proteins. Furthermore, this region is predicted to adopt an amphiphilic alpha-helical conformation similar to that of mitochondrial signal peptides. Conservation of that sequence and of other segments of the end domains of EndoA supports the idea that those regions are implicated in the specific organization of the IF network in the cell and in the interactions of IF with other cell constituents.
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