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  Amino acid sequences and homopolymer-forming ability of the intermediate filament proteins from an invertebrate epithelium.

Weber, K., Plessmann, U., Dodemont, H., & Kossmagk-Stephan, K. (1988). Amino acid sequences and homopolymer-forming ability of the intermediate filament proteins from an invertebrate epithelium. EMBO Journal, 7(10), 2995-3001.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-439F-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-43A1-3
Genre: Journal Article

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 Creators:
Weber, K.1, Author              
Plessmann, U.1, Author              
Dodemont, H.1, Author              
Kossmagk-Stephan, K.1, Author              
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1Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              

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 Abstract: Intermediate filaments (IF) isolated from the oesophagus epithelium of the snail Helix pomatia contain two polypeptides of mol. wt 66,000 (A) and 52,000 (B), which we have now characterized by in vitro self-assembly studies and by protein sequences. A and B can each form morphologically normal IF and share extended regions of sequence identity. All A-specific sequences seem to locate to an extension of the carboxyl-terminal domain. Although the Helix protein(s) reveal the IF-consensus sequences at the ends of the coiled-coil, the remainder of the rod domain shows conservation of sequence principles rather than extended homology, when compared with any subtype of vertebrate IF proteins. Interestingly, the Helix proteins have the longer coil 1b domain found in nuclear lamins and not in cytoplasmic IF proteins of vertebrates. They lack, however, the karyophilic signal sequence typical for lamins. Obvious implications for IF evolution and structure are discussed.

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Language(s): eng - English
 Dates: 1988-10
 Publication Status: Published in print
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Title: EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 7 (10) Sequence Number: - Start / End Page: 2995 - 3001 Identifier: -