Linked Life Data

10801351

Source:http://linkedlifedata.com/resource/pubmed/id/10801351

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-6-14
pubmed:abstractText
Nearly all intermediate filament proteins exhibit a highly conserved amino acid 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
298
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
817-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10801351-Amino Acid Motifs, pubmed-meshheading:10801351-Amino Acid Sequence, pubmed-meshheading:10801351-Animals, pubmed-meshheading:10801351-Consensus Sequence, pubmed-meshheading:10801351-Crystallography, X-Ray, pubmed-meshheading:10801351-Desmin, pubmed-meshheading:10801351-Hydrogen-Ion Concentration, pubmed-meshheading:10801351-Intermediate Filament Proteins, pubmed-meshheading:10801351-Mice, pubmed-meshheading:10801351-Microscopy, Electron, Scanning Transmission, pubmed-meshheading:10801351-Models, Molecular, pubmed-meshheading:10801351-Molecular Sequence Data, pubmed-meshheading:10801351-Molecular Weight, pubmed-meshheading:10801351-Osmolar Concentration, pubmed-meshheading:10801351-Peptide Fragments, pubmed-meshheading:10801351-Protein Binding, pubmed-meshheading:10801351-Protein Structure, Secondary, pubmed-meshheading:10801351-Protein Structure, Tertiary, pubmed-meshheading:10801351-Recombinant Fusion Proteins, pubmed-meshheading:10801351-Sequence Alignment, pubmed-meshheading:10801351-Ultracentrifugation, pubmed-meshheading:10801351-Vimentin, pubmed-meshheading:10801351-Viscosity, pubmed-meshheading:10801351-Xenopus laevis
pubmed:year
2000
pubmed:articleTitle
The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly.
pubmed:affiliation
Division of Cell Biology, German Cancer Research Center, Im Neuenheimer Feld 280, Heidelberg, D-69120, Germany. h.herrmann@dkfz.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't