ArticleThe EMBO journal1987
Analysis of cytokeratin domains by cloning and expression of intact and deleted polypeptides in Escherichia coli.
Article in The EMBO journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 67 citations in OpenAlex.
- The monoclonal antibody EPR1614Y against the stem cell biomarker keratin K15 lacks specificity and reacts with other keratins.Scientific reports · 2019Article
- Lessons from keratin 18 knockout mice: formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates.The Journal of cell biology · 1998Article
- Gene targeting at the mouse cytokeratin 10 locus: severe skin fragility and changes of cytokeratin expression in the epidermis.The Journal of cell biology · 1996Article
- A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments.The Journal of cell biology · 1992Article
- Intermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus.The Journal of cell biology · 1991Article
- A potential role for the COOH-terminal domain in the lateral packing of type III intermediate filaments.The Journal of cell biology · 1991Article
- Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions.The Journal of cell biology · 1991Article
- The use of sarkosyl in generating soluble protein after bacterial expression.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Identification of protein IT of the intestinal cytoskeleton as a novel type I cytokeratin with unusual properties and expression patterns.The Journal of cell biology · 1990Article
- Elucidating the early stages of keratin filament assembly.The Journal of cell biology · 1990Article
- A polypeptide of 59 kDa is associated with bundles of cytoplasmic filaments in Neurospora crassa.The Biochemical journal · 1990Article
- The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression.The Journal of cell biology · 1990Article
- Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode.The EMBO journal · 1989Article
- Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8.Molecular and cellular biology · 1989Article
- Amino acid sequences and homopolymer-forming ability of the intermediate filament proteins from an invertebrate epithelium.The EMBO journal · 1988Article
- Molecular characterization and expression of the stratification-related cytokeratins 4 and 15.The Journal of cell biology · 1988Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using recombination of an appropriate expression vector system (pINDU) with a complete cDNA encoding a basic (type II) cytokeratin, i.e. cytokeratin 8 (1) of Xenopus laevis, we transformed Escherichia coli cells to synthesize considerable amounts of an insoluble eukaryotic cytoskeletal protein. The cytokeratin was deposited in large 'inclusion bodies' in the bacterial cytoplasm but did not form detectable filamentous structures. However, when the E. coli-expressed cytokeratin was purified and combined in vitro with an authentic cytokeratin of the complementary, i.e. acidic (type I) subfamily, it formed typical intermediate-sized filaments (IFs). Using Bal31 deletion from either the 5' or the 3' end of the cDNA, series of polypeptides progressively deleted from the amino or the carboxy terminus were produced in E. coli and identified by monoclonal antibodies. These assays allowed the mapping of epitopes. The deletion polypeptides of cytokeratin 8 were further examined to localize the region(s) involved in the heterotypic binding of alpha-helices of type I cytokeratins, using an in vitro nitrocellulose blot binding assay. We show that a region of 37 amino acids located in the central portion of coil 2 of the alpha-helical rod domain is sufficient for the specific recognition of a radiolabelled type I cytokeratin, i.e. cytokeratin 18 (D) from rat liver. In addition, deletion polypeptides containing only coil 1 of the alpha-helical rod also bind strongly the complementary cytokeratin. This indicates that the capability of heterotypic recognition and complex formation is not restricted to a single signal sequence but is located in distant and independent alpha-helical domains.(ABSTRACT TRUNCATED AT 250 WORDS)
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