Organization of the coiled-coils in the wool microfibril

Woods, E. F.; Inglis, A.S.

doi:10.1016/0141-8130(84)90008-4

Cited by 71 publications

(36 citation statements)

References 31 publications

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“…4). This model is consistent with earlier observations, derived from proteolysis studies, that helix 1B could be isolated as a tetramer (Gruen and Woods, 1981;Woods and Inglis, 1984). In an extensive series of chemical crosslinking studies on keratin pairs (Steinert et al, 1993a(Steinert et al, , 1993b and vimentin (Steinert et al, 1993c), Steinert and co-workers identified a number of lysine-lysine and cysteine-cysteine cross-links, which led them to describe four types of domain alignment termed A 11 , A 22 , A 12 , and A CN (Fig.…”

Section: Discussionsupporting

confidence: 74%

“…Accompanying Western blotting experiments showed that helices 1B form tetramers, consistent with the aforementioned observation that helix 1 tetramers could be isolated from proteolyzed wool keratin (Gruen and Woods, 1981;Woods and Inglis, 1984). Thus, we conclude that helix 1B is a site along the molecule at which active interaction occurs to stabilize the structure of an IF.…”

Section: Discussionsupporting

confidence: 65%

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Intermediate Filament Protein Domain Interactions as Revealed by Two-hybrid Screens

Meng

Khan

1996

Journal of Biological Chemistry

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All intermediate filament proteins possess three distinct domains: heads, rod and tail, and subdomains within the rod called helices 1A, 1B, 2A, and 2B. Subunit packing within a filament is a consequence of interactions among these domains. Several such interactions are known, but probably many more contribute to stabilizing filament structure. We examined a number of such potential interactions using the yeast two-hybrid system. Domains or subdomains of murine vimentin, a Type III intermediate filament protein, were fused with either the DNA-binding or trans-activating domain of GAL4, a transcription factor. Interaction between the vimentin domains/subdomains functionally reconstituted GAL4, thereby activating transcription of a GAL1-LacZ reporter gene. The oligomeric state at which the interactions took place, i.e. whether the domains/subdomains were dimeric or tetrameric as they interacted, was also determined. These studies revealed a number of interesting interactions, among which was a strong homotypic binding of helix 2B to form tetramers. They also demonstrated a lack of interaction among others expected to do so based on current structural models. From these results we deduced which of the candidates for interactions, suggested by current models, were true protein-protein interactions and which represented nearest-neighbors only. Thus, the A 11 and A 22 modes of molecular alignment identified by Steinert et al.

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Section: Discussionsupporting

confidence: 74%

Section: Discussionsupporting

confidence: 65%

Intermediate Filament Protein Domain Interactions as Revealed by Two-hybrid Screens

Meng

Khan

1996

Journal of Biological Chemistry

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“…The helices contain heptad repeats of hydrophobic residues, producing a hydrophobic seal on the helical surface, enabling the coiled-coil heterodimerization of in register, parallelly aligned molecules of K5 and K14, or Kl and KIO (5)(6)(7). In vitro, dimers associate in antiparallel fashion to form two types of tetramers: a form where the amino ends of two dimers overlap in a near half-staggered alignment and an unstaggered form (8)(9)(10)(11). IFs are ropelike in structure, with putative strings of tetramers forming protofilaments, which intertwine to form protofibrils, which in turn intertwine to yield a single 10-nm filament (12)(13)(14).…”

Section: Introductionmentioning

confidence: 99%

Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity.

Syder

Paller³

et al. 1994

J. Clin. Invest.

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Epidermolytic hyperkeratosis (EH) is a skin disease caused by mutations in the genes encoding K1 and K10, the differentiation-specific keratins of epidermis. To explore the heterogeneity of mutations and to assess whether a correlation exists between disease severity and the extent to which a mutation interferes with keratin network formation, we determined the genetic bases of four severe incidences of EH and one unusually mild case. Two severe cases have the same mutation, K10-R156:C, at a conserved arginine that we previously showed was mutated to a histidine in two unrelated EH families. An additional severe case has a mutation six residues away, still within the amino end of the a-helical rod domain of K10. The other severe case has a mutation in the conserved carboxy end of the K1 rod. In contrast, affected members of the atypically mild family have a mutation just proximal to the conserved carboxy end of the K10 rod. By genetic engineering and gene transfection, we demonstrate that each mutation is functionally responsible for the keratin filament aberrations that are typical of keratinocytes cultured from these patients. Moreover, we show that the mild EH mutation less severely affects filament network formation. Taken together, our studies strengthen the link between filament perturbations, cell fragility, and degeneration. (J. Clin. Invest. 1994.93:1533-1542

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“…1 for the nomenclature used to designate the various segments). Several lines of evidence suggest that the chains are parallel in the two-strand rope segments and in axial register (3,4,9).…”

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confidence: 99%

Intermediate filaments in alpha-keratins.

Fraser¹,

MacRae²,

Parry³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Previous x-ray diffraction studies on the alpha-keratins of hair and wool have revealed that the intermediate filaments (IF) have a helical structure rendered imperfect by a precisely defined dislocation. It has also been possible to deduce a surface lattice for the IF and to determine the number of IF molecules associated with each lattice point. In this work this information is combined with data on the ionic interactions between the coiled-coil rope segments of the IF molecules to provide a plausible model for the pattern of interactions that stabilize the framework of the IF in the "hard" alpha-keratins. Similar interaction studies of the proteins from the IF in the so-called "soft" alpha-keratin from the stratum corneum layer of the skin suggest that they are likely to have an essentially similar pattern.

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Organization of the coiled-coils in the wool microfibril

Cited by 71 publications

References 31 publications

Intermediate Filament Protein Domain Interactions as Revealed by Two-hybrid Screens

Intermediate Filament Protein Domain Interactions as Revealed by Two-hybrid Screens

Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity.

Intermediate filaments in alpha-keratins.

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