Literature DB >> 6188504

Structural homology between hard alpha-keratin and the intermediate filament proteins desmin and vimentin.

L M Dowling, D A Parry, L G Sparrow.   

Abstract

Although it has been assumed that the microfibrils in hard -keratin are members of the class of structures known as intermediate filaments (IF), no firm chemical evidence relating the low-sulfur proteins in hard -keratin to other IF proteins has yet been published. We now present primary sequence data for two components from wool keratin which show striking similarities with two IF proteins, desmin and vimentin. The sequences show marked homology, a heptad repeat and a 9.5-residue periodicity in the linear disposition of the acidic and the basic residues. These data thus provide the first evidence that the low-sulfur proteins in hard -keratin and the other IF proteins do indeed have both a similar structure and a common evolutionary origin.

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Year:  1983        PMID: 6188504     DOI: 10.1007/bf01121573

Source DB:  PubMed          Journal:  Biosci Rep        ISSN: 0144-8463            Impact factor:   3.840


  16 in total

1.  Secondary structure of component 8c-1 of alpha-keratin. An analysis of the amino acid sequence.

Authors:  L M Dowling; W G Crewther; D A Parry
Journal:  Biochem J       Date:  1986-06-15       Impact factor: 3.857

2.  The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments.

Authors:  L M Dowling; W G Crewther; A S Inglis
Journal:  Biochem J       Date:  1986-06-15       Impact factor: 3.857

3.  Complete sequence of a gene encoding a human type I keratin: sequences homologous to enhancer elements in the regulatory region of the gene.

Authors:  D Marchuk; S McCrohon; E Fuchs
Journal:  Proc Natl Acad Sci U S A       Date:  1985-03       Impact factor: 11.205

4.  The amino acid sequence of component 7c, a type II intermediate-filament protein from wool.

Authors:  L G Sparrow; C P Robinson; D T McMahon; M R Rubira
Journal:  Biochem J       Date:  1989-08-01       Impact factor: 3.857

5.  The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 Da: analysis of sequence differences between type I and type II keratins.

Authors:  P M Steinert; D A Parry; E L Racoosin; W W Idler; A C Steven; B L Trus; D R Roop
Journal:  Proc Natl Acad Sci U S A       Date:  1984-09       Impact factor: 11.205

6.  Mammalian keratin gene families: organisation of genes coding for the B2 high-sulphur proteins of sheep wool.

Authors:  B C Powell; M J Sleigh; K A Ward; G E Rogers
Journal:  Nucleic Acids Res       Date:  1983-08-25       Impact factor: 16.971

Review 7.  Inroads into the structure and function of intermediate filament networks.

Authors:  Robert D Goldman; Megan M Cleland; S N Prasanna Murthy; Saleemulla Mahammad; Edward R Kuczmarski
Journal:  J Struct Biol       Date:  2011-11-18       Impact factor: 2.867

8.  Neurofilament architecture combines structural principles of intermediate filaments with carboxy-terminal extensions increasing in size between triplet proteins.

Authors:  N Geisler; E Kaufmann; S Fischer; U Plessmann; K Weber
Journal:  EMBO J       Date:  1983       Impact factor: 11.598

9.  Protein-chemical characterization of NF-H, the largest mammalian neurofilament component; intermediate filament-type sequences followed by a unique carboxy-terminal extension.

Authors:  N Geisler; S Fischer; J Vandekerckhove; J V Damme; U Plessmann; K Weber
Journal:  EMBO J       Date:  1985-01       Impact factor: 11.598

10.  Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non-epithelial members.

Authors:  N Geisler; K Weber
Journal:  EMBO J       Date:  1983       Impact factor: 11.598

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