TY - JOUR
T1 - The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins
AU - Hanukoglu, Israel
AU - Fuchs, Elaine
N1 - Funding Information:
All materials and methods used for thus study are stmtlar to those we prevrously used tn the sequenctng and analysis of the 50 K Type I keratin cDNA sequence (Hanukoglu and Fuchs, 1982). In bnef, the DNA sequence analysrs was camed out according to the procedure of Maxam and Gilbert (1980). The purificatton and amino acid analysis of the 56 K keratin was camed out as prevtously described (Hanukoglu and Fuchs, 1982). The predtctron of the secondary structures of the different IF proterns accordrng to the method of Gamier. Osguthorpe, and Robson (1978) was done ustng a computer program we obtained from B. Robson (Universrty of Manchester). For the prediction of the secondary structures of these proteins according to the method of Chou and Fasman (1978; 1979a), we used a program written by one of us We are grateful to Naoko Tanese and Joan Harper for therr very capable technical asststance. In additron we gratefully acknowledge that we used the Stanford Untverstty Molgen Protect resources for DNA sequence anal-ysls I. H. IS the rectpient of a National Research Servtce Award #lF32-CA07145. E. F. is a Searle Scholar and the recipient of a Research Career Development Award #lKO4-AMOO997. This work was supported by National Institutes of Health grant 1 ROl -AM278&3.
PY - 1983/7
Y1 - 1983/7
N2 - We present the cDNA and amino acid sequences of a cytoskeletal keratin from human epidermis (Mr = 56K) that belongs to one of the two classes of keratins (Type I and Type II) present in all vertebrates. In these two types of keratins the central ∼300 residue long regions share ∼30% homology both with one another and with the sequences of other IF proteins. Within this region, all IF proteins are predicted to contain four helical domains demarcated from one another by three regions of β-turns. The amino and carboxy termini of the Type II keratin are very different from those of microfibrillar keratins and other nonkeratin IF proteins. However, they contain unusual glycine-rich tandem repeats similar to the amino terminus of the Type I keratin. Thus the size heterogeneity among keratins appears to be a result of differences in the length of the terminal ends rather than the structurally conserved central region.
AB - We present the cDNA and amino acid sequences of a cytoskeletal keratin from human epidermis (Mr = 56K) that belongs to one of the two classes of keratins (Type I and Type II) present in all vertebrates. In these two types of keratins the central ∼300 residue long regions share ∼30% homology both with one another and with the sequences of other IF proteins. Within this region, all IF proteins are predicted to contain four helical domains demarcated from one another by three regions of β-turns. The amino and carboxy termini of the Type II keratin are very different from those of microfibrillar keratins and other nonkeratin IF proteins. However, they contain unusual glycine-rich tandem repeats similar to the amino terminus of the Type I keratin. Thus the size heterogeneity among keratins appears to be a result of differences in the length of the terminal ends rather than the structurally conserved central region.
UR - http://www.scopus.com/inward/record.url?scp=0020614212&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(83)90034-X
DO - 10.1016/0092-8674(83)90034-X
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C2 - 6191871
AN - SCOPUS:0020614212
SN - 0092-8674
VL - 33
SP - 915
EP - 924
JO - Cell
JF - Cell
IS - 3
ER -