Assembly and architecture of invertebrate cytoplasmic intermediate filaments reconcile features of vertebrate cytoplasmic and nuclear lamin-type intermediate filaments
Identifieur interne : 002577 ( Istex/Curation ); précédent : 002576; suivant : 002578Assembly and architecture of invertebrate cytoplasmic intermediate filaments reconcile features of vertebrate cytoplasmic and nuclear lamin-type intermediate filaments
Auteurs : Norbert Geisler [Allemagne] ; Jürgen Schünemann [Allemagne] ; Klaus Weber [Allemagne] ; Markus H Ner [Suisse] ; Ueli Aebi [Suisse]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1998.
English descriptors
- KwdEn :
- Teeft :
- Academic press, Additional salt, Aebi, Amino acid residue, Anneal, Anneal longitudinally, Antiparallel, Appropriate conditions, Arrowhead, Ascaris, Ascaris oligomer buffer, Ascaris proteins, Assembly conditions, Assembly figure, Axial, Bartnik, Beading, Biol, Biotinylated proteins, Buffer conditions, Cell biol, Central pairs, Cytoplasmic, Desmin, Different types, Dimer, Dimer rods, Dodemont, Domain, Electron micrographs, Equal amounts, Filament, Geisler, Globular, Globular domains, Globular tail domains, Globular tails, Globule, Head domain, Head domains, Heins, Heitlinger, Helix, Helix oligomer buffer, Helix proteins, Herrmann, Herrmann aebi, High protein, Intermediate filament structure, Invertebrate, Invertebrate cytoplasmic, Ionic strength, Lament, Lament assembly, Lament buffer, Lament formation, Lament proteins, Lament structure, Lamin, Lamin dimers, Lamins, Last residue, Lateral, Lateral association, Laterally, Longitudinally, Micrographs, Negative staining, Nematode ascaris suum, Nuclear lamins, Octamer, Octameric, Octamers, Oligomer, Oligomers, Polymerization behaviour, Polymerization characteristics, Polymerized, Polypeptide, Protein, Protein pairs, Protostomic, Protostomic invertebrate, Residue insertion, Same mechanism, Scale bars, Schematic representation, Small oligomers, Smaller globules, Snail helix pomatia, Tail domain, Tail domains, Tetramer, Tetramers, Tetramers anneal longitudinally, Vertebrate, Vertebrate cytoplasmic, Vimentin, Weber, Xenopus vimentin.
Abstract
Abstract: The two major intermediate filament (IF) proteins from the esophagus epithelium of the snail Helix pomatia and the two major IF proteins from muscle tissue of the nematode Ascaris suum were investigated under a variety of assembly conditions. The lowest-order complexes from each of the four protostomic invertebrate (p-INV) IF proteins are parallel, unstaggered dimers involving two-stranded α-helical coiled coil formation of their ∼350 amino acid residue central rod domain (i.e. long-rod). In the electron microscope these are readily recognized by their distinct ∼56 nm long rod with two globular domains (i.e. representing the non-helical carboxy-terminal tail domain of the p-INV IF proteins) attached at one end, closely resembling vertebrate lamin dimers. The next-higher-order oligomers are tetramers, which are easily recognized by their two pairs of globular tail domains attached at either end of a ∼72 nm long central rod portion. According to their size and shape, these tetramers are built from two dimers associated laterally in an antiparallel, approximately half-staggered fashion via the amino-terminal halves of their rod domains. This is similar to the NN-type tetramers found as the most abundant oligomer species in all types of vertebrate cytoplasmic IF proteins, which contain a ∼310 amino acid residue central rod domain (i.e. short-rod). As a first step toward filament formation, the p-INV IF tetramers anneal longitudinally into protofilaments by antiparallel CC-type association of the carboxy-terminal halves of their dimer rods. The next step involves radial growth, occurring initially through lateral association of two four-chain protofilaments into octameric subfibrils, which then further associate into mature, full-width filaments. Head-to-tail polymers of dimers and paracrystalline fibers commonly observed with vertebrate lamins were only rarely seen with p-INV IF proteins. The globular domains residing at the carboxy-terminal end of p-INV IF dimers were studding the surface of the filaments at regular, ∼24.5 nm intervals, thereby giving them a “beaded” appearance with an axial periodicity of about 24.5 nm, which is ∼3 nm longer than the corresponding ∼21.5 nm repeat pattern exhibited by short-rod vertebrate IFs.
Url:
DOI: 10.1006/jmbi.1998.1995
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<series><title level="j">Journal of Molecular Biology</title>
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<term>IF</term>
<term>MPL</term>
<term>NN</term>
<term>STEM</term>
<term>filament assembly</term>
<term>intermediate filaments (IFs)</term>
<term>nuclear lamins</term>
<term>p-INV</term>
<term>protostomic invertebrate IFs</term>
<term>structural biology</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Academic press</term>
<term>Additional salt</term>
<term>Aebi</term>
<term>Amino acid residue</term>
<term>Anneal</term>
<term>Anneal longitudinally</term>
<term>Antiparallel</term>
<term>Appropriate conditions</term>
<term>Arrowhead</term>
<term>Ascaris</term>
<term>Ascaris oligomer buffer</term>
<term>Ascaris proteins</term>
<term>Assembly conditions</term>
<term>Assembly figure</term>
<term>Axial</term>
<term>Bartnik</term>
<term>Beading</term>
<term>Biol</term>
<term>Biotinylated proteins</term>
<term>Buffer conditions</term>
<term>Cell biol</term>
<term>Central pairs</term>
<term>Cytoplasmic</term>
<term>Desmin</term>
<term>Different types</term>
<term>Dimer</term>
<term>Dimer rods</term>
<term>Dodemont</term>
<term>Domain</term>
<term>Electron micrographs</term>
<term>Equal amounts</term>
<term>Filament</term>
<term>Geisler</term>
<term>Globular</term>
<term>Globular domains</term>
<term>Globular tail domains</term>
<term>Globular tails</term>
<term>Globule</term>
<term>Head domain</term>
<term>Head domains</term>
<term>Heins</term>
<term>Heitlinger</term>
<term>Helix</term>
<term>Helix oligomer buffer</term>
<term>Helix proteins</term>
<term>Herrmann</term>
<term>Herrmann aebi</term>
<term>High protein</term>
<term>Intermediate filament structure</term>
<term>Invertebrate</term>
<term>Invertebrate cytoplasmic</term>
<term>Ionic strength</term>
<term>Lament</term>
<term>Lament assembly</term>
<term>Lament buffer</term>
<term>Lament formation</term>
<term>Lament proteins</term>
<term>Lament structure</term>
<term>Lamin</term>
<term>Lamin dimers</term>
<term>Lamins</term>
<term>Last residue</term>
<term>Lateral</term>
<term>Lateral association</term>
<term>Laterally</term>
<term>Longitudinally</term>
<term>Micrographs</term>
<term>Negative staining</term>
<term>Nematode ascaris suum</term>
<term>Nuclear lamins</term>
<term>Octamer</term>
<term>Octameric</term>
<term>Octamers</term>
<term>Oligomer</term>
<term>Oligomers</term>
<term>Polymerization behaviour</term>
<term>Polymerization characteristics</term>
<term>Polymerized</term>
<term>Polypeptide</term>
<term>Protein</term>
<term>Protein pairs</term>
<term>Protostomic</term>
<term>Protostomic invertebrate</term>
<term>Residue insertion</term>
<term>Same mechanism</term>
<term>Scale bars</term>
<term>Schematic representation</term>
<term>Small oligomers</term>
<term>Smaller globules</term>
<term>Snail helix pomatia</term>
<term>Tail domain</term>
<term>Tail domains</term>
<term>Tetramer</term>
<term>Tetramers</term>
<term>Tetramers anneal longitudinally</term>
<term>Vertebrate</term>
<term>Vertebrate cytoplasmic</term>
<term>Vimentin</term>
<term>Weber</term>
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<front><div type="abstract" xml:lang="en">Abstract: The two major intermediate filament (IF) proteins from the esophagus epithelium of the snail Helix pomatia and the two major IF proteins from muscle tissue of the nematode Ascaris suum were investigated under a variety of assembly conditions. The lowest-order complexes from each of the four protostomic invertebrate (p-INV) IF proteins are parallel, unstaggered dimers involving two-stranded α-helical coiled coil formation of their ∼350 amino acid residue central rod domain (i.e. long-rod). In the electron microscope these are readily recognized by their distinct ∼56 nm long rod with two globular domains (i.e. representing the non-helical carboxy-terminal tail domain of the p-INV IF proteins) attached at one end, closely resembling vertebrate lamin dimers. The next-higher-order oligomers are tetramers, which are easily recognized by their two pairs of globular tail domains attached at either end of a ∼72 nm long central rod portion. According to their size and shape, these tetramers are built from two dimers associated laterally in an antiparallel, approximately half-staggered fashion via the amino-terminal halves of their rod domains. This is similar to the NN-type tetramers found as the most abundant oligomer species in all types of vertebrate cytoplasmic IF proteins, which contain a ∼310 amino acid residue central rod domain (i.e. short-rod). As a first step toward filament formation, the p-INV IF tetramers anneal longitudinally into protofilaments by antiparallel CC-type association of the carboxy-terminal halves of their dimer rods. The next step involves radial growth, occurring initially through lateral association of two four-chain protofilaments into octameric subfibrils, which then further associate into mature, full-width filaments. Head-to-tail polymers of dimers and paracrystalline fibers commonly observed with vertebrate lamins were only rarely seen with p-INV IF proteins. The globular domains residing at the carboxy-terminal end of p-INV IF dimers were studding the surface of the filaments at regular, ∼24.5 nm intervals, thereby giving them a “beaded” appearance with an axial periodicity of about 24.5 nm, which is ∼3 nm longer than the corresponding ∼21.5 nm repeat pattern exhibited by short-rod vertebrate IFs.</div>
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