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Titolo:
The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly
Autore:
Herrmann, H; Strelkov, SV; Feja, B; Rogers, KR; Brettel, M; Lustig, A; Haner, M; Parry, DAD; Steinert, PM; Burkhard, P; Aebi, U;
Indirizzi:
German Canc Res Ctr, Div Cell Biol, D-69120 Heidelberg, Germany German Canc Res Ctr Heidelberg Germany D-69120 69120 Heidelberg, Germany Univ Basel, Biozentrum, Maurice E Miller Inst, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 er Inst, CH-4056 Basel, Switzerland Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand Massey Univ Palmerston North New Zealand Palmerston North, New Zealand NIAMS, Skin Biol Lab, NIH, Bethesda, MD 20892 USA NIAMS Bethesda MD USA 20892 S, Skin Biol Lab, NIH, Bethesda, MD 20892 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 5, volume: 298, anno: 2000,
pagine: 817 - 832
SICI:
0022-2836(20000519)298:5<817:TIFPCM>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEMATODE CAENORHABDITIS-ELEGANS; NUCLEAR LAMIN; COILED-COIL; IF PROTEINS; IN-VITRO; MOLECULAR CHARACTERISTICS; MASS DETERMINATION; ESCHERICHIA-COLI; SIZED FILAMENTS; TAIL DOMAIN;
Keywords:
intermediate filament protein; assembly; atomic structure; vimentin; desmin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Herrmann, H German Canc Res Ctr, Div Cell Biol, Neuenheimer Feld 280, D-69120 Heidelberg, Germany German Canc Res Ctr Neuenheimer Feld 280 Heidelberg Germany D-69120
Citazione:
H. Herrmann et al., "The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly", J MOL BIOL, 298(5), 2000, pp. 817-832

Abstract

Nearly all intermediate filament proteins exhibit a highly conserved aminoacid motif (YRKLLEGEE) at the C-terminal end of their central alpha-helical rod domain. We have analyzed its contribution to the various stages of assembly by using truncated forms of Xenopus vimentin and mouse desmin, VimIAT and DesIAT, which terminate exactly before this motif, by comparing them with the wild-type and tailless proteins. It is surprising that in buffers of low ionic strength and high pH where the full-length proteins form tetramers, both VimIAT and DesIAT associated into various high molecular weight complexes. After initiation of assembly, both VimIAT and DesIAT aggregated into unit-length-type filaments, which rapidly longitudinally annealed to yield filaments of around 20 nm in diameter. Mass measurements by scanning transmission electron microscopy revealed that both VimIAT and DesIAT filaments contained considerably more subunits per cross-section than standard intermediate filaments. This indicated that the YRKLLEGEE-motif is crucial for the formation of authentic tetrameric complexes and also for the control of filament width, rather than elongation, during assembly. To determine the structure of the YRKLLEGEE domain, we grew crystals of peptides containing the last 28 amino acid residues of coil 2B, chimerically fused at its amino-terminal end to the 31 amino acid-long leucine zipper domain of the yeast transcription factor GCN4 to facilitate appropriate coiled-coil formation. The atomic structure shows that starting from Tyr400 the two helices gradually separate and that the coiled coil terminates with residue Glu405 while the downstream residues fold away from the coiled-coil axis. (C) 2000 Academic Press.

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Documento generato il 04/04/20 alle ore 11:04:59