InteractionIn Vitroof Type III Intermediate Filament Proteins with Z-DNA and B-Z-DNA Junctions

2003 ◽  
Vol 22 (3) ◽  
pp. 141-169 ◽  
Author(s):  
Guohong Li ◽  
Genrich V. Tolstonog ◽  
Peter Traub
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Type Iii ◽  
Dna Junctions ◽  
Z Dna

scholarly journals Common and variant properties of intermediate filament proteins from lower chordates and vertebrates; two proteins from the tunicate Styela and the identification of a type III homologue

1998 ◽  
Vol 111 (19) ◽  
pp. 2967-2975
Author(s):  
D. Riemer ◽  
K. Weber
Keyword(s):  
Intermediate Filament ◽  
Self Assembly ◽  
Expression Patterns ◽  
Intron Position ◽  
Gene Organization ◽  
The Body ◽  
Specific Expression ◽  
Intermediate Filament Proteins ◽  
Type Iii

The chordates combine the vertebrates and the invertebrate phyla of the cephalo- and urochordates (tunicates). Two cytoplasmic intermediate filament (IF) proteins of the urochordate Styela plicata are characterized by cDNA cloning, gene organization, tissue specific expression patterns in the adult animal and the self assembly properties of the recombinant proteins. In line with metazoan phylogeny St-A and St-B have the short length version of the coil 1b domain found in all vertebrate and cephalochordate IF proteins while protostomic IF proteins have the longer length version with an extra 42 residues. St-A is the first IF protein from a lower chordate which can be unambiguously related to a particular vertebrate IF subfamily. St-A shares 46% sequence identity with desmin, displays the N-terminal motif necessary for filament assembly of type III proteins and forms normal homopolymeric 10 nm filaments in vitro. St-A but not St-B is present in smooth muscle cells of the body wall musculature. St-A and St-B are found as separate networks in some interior epithelia. St-B shares 30 to 35% identity with keratin 8, St-A and desmin and does not form IF under in vitro assembly conditions. Its relation to a particular vertebrate IF type or to the eight currently known IF proteins from the cephalochordate Branchiostoma remains unresolved. The striking relation between St-A and desmin predicts that the common progenitor of the urochordate (tunicate) and the cephalochordate/vertebrate lineages already possessed a type III homologue. Unlike in vertebrates intron patterns cannot be used to classify the tunicate IF genes. Although St-A is a type III homologue its gene shows an intron position which in vertebrates is restricted to keratin type II genes.

Identification of two N-terminal non-alpha-helical domain motifs important in the assembly of glial fibrillary acidic protein

1994 ◽  
Vol 107 (7) ◽  
pp. 1935-1948 ◽  
Author(s):  
J.E. Ralton ◽  
X. Lu ◽  
A.M. Hutcheson ◽  
R.A. Quinlan
Keyword(s):  
Intermediate Filament ◽  
Consensus Sequence ◽  
Intermediate Filament Protein ◽  
Intermediate Filament Proteins ◽  
Type Iii ◽  
Conserved Sequence ◽  
Terminal Domain ◽  
Filament Assembly ◽  
Arginine Residues ◽  
Filament Protein

The non-alpha-helical N-terminal domain of intermediate filament proteins plays a key role in filament assembly. Previous studies have identified a nonapeptide motif, SSYRRIFGG, in the non-alpha-helical N-terminal domain of vimentin that is required for assembly. This motif is also found in desmin, peripherin and the type IV intermediate filament proteins. GFAP is the only type III intermediate filament protein in which this motif is not readily identified. This study has identified two motifs in the non-alpha-helical N-terminal domain of mouse GFAP that play important roles in GFAP assembly. One motif is located at the very N terminus and has the consensus sequence, MERRRITS-ARRSY. It has some characteristics in common with the vimentin nonapeptide motif, SSYRRIFGG, including its location in the non-alpha-helical N-terminal domain and a concentration of arginine residues. Unlike the vimentin motif in which even conserved sequence changes affect filament assembly, the GFAP consensus sequence, MERRRITS-ARRSY, can be replaced by a completely unrelated sequence; namely, the heptapeptide, MVRANKR, derived from the lambda cII protein. When fused to GFAP sequences with sequential deletions of the N-terminal domain, the lambda cII heptapeptide was used to help identify a second motif, termed the RP-box, which is located just upstream of the GFAP alpha-helical rod domain. This RP-box affected the efficiency of filament assembly as well as protein-protein interactions in the filament, as shown by sedimentation assays and electron microscopy. These results are supported by previous data, which showed that the dramatic reorganization of GFAP within cells was due to phosphorylation-dephosphorylation of a site located in this RP-box. The results in this study suggest the RP-box motif to be a key modulator in the mechanism of GFAP assembly, and support a role for this motif in both the nucleation and elongation phases of filament assembly. The RP-box motif in GFAP has the consensus sequence, RLSL-RM-PP. Sequences similar to the GFAP RP-box motif are also to be found in vimentin, desmin and peripherin. Like GFAP, these include phosphorylation and proteolysis sites and are adjacent to the start of the central alpha-helical rod domain, suggesting that this motif of general importance to type III intermediate filament protein assembly.

scholarly journals Elucidation of GlcNAc-binding properties of type III intermediate filament proteins, using GlcNAc-bearing polymers

2017 ◽  
Vol 22 (10) ◽  
pp. 900-917 ◽  
Author(s):  
Hirohiko Ise ◽  
Sadanori Yamasaki ◽  
Kazuaki Sueyoshi ◽  
Yoshiko Miura
Keyword(s):  
Intermediate Filament ◽  
Binding Properties ◽  
Intermediate Filament Proteins ◽  
Type Iii

Plectin interacts with the rod domain of type III intermediate filament proteins desmin and vimentin

2011 ◽  
Vol 90 (5) ◽  
pp. 390-400 ◽  
Author(s):  
Bertrand Favre ◽  
Yann Schneider ◽  
Prakash Lingasamy ◽  
Jamal-Eddine Bouameur ◽  
Nadja Begré ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Type Iii

The endless story of the glial fibrillary acidic protein

1994 ◽  
Vol 107 (8) ◽  
pp. 2299-2311 ◽  
Author(s):  
W.J. Chen ◽  
R.K. Liem
Keyword(s):  
Glial Fibrillary Acidic Protein ◽  
Intermediate Filament ◽  
Self Assembly ◽  
Acidic Protein ◽  
Terminal Deletion ◽  
Deletion Mutants ◽  
Tail Domain ◽  
Intermediate Filament Proteins ◽  
Type Iii ◽  
Head Domain

All intermediate filament proteins consist of an alpha-helical rod domain flanked by non-helical N-terminal head and C-terminal tail domains. The roles of the non-helical domains of various intermediate filament proteins in the assembly and co-assembly of higher-order filamentous structures have been studied by many groups but with quite contradictory results. Type III intermediate filaments are unique in that they can form homopolymers both in vitro and in vivo. The expression and assembly characteristics of carboxy- and amino-terminal deletion mutants of glial fibrillary acidic protein (GFAP), an astrocyte-specific type III intermediate filament protein, were examined by transient transfections of either vimentin-positive or vimentin-negative variants of human adrenocarcinoma-derived SW13 cell lines. Whereas complete deletion of the C-terminal tail domain of GFAP results in the formation of polymorphic aggregates, both intranuclear and cytoplasmic in self-assembly experiments, efficient co-assembly of these tail-less GFAP mutants with vimentin can be achieved as long as the KLLEGEE sequence at the C-terminal end of the rod domain is preserved. Up to one-fifth of the C-terminal end of the tail domain can be deleted without affecting the capability of GFAP to self-assemble. The highly conserved RDG-containing motif in the tail domain may be important for self-assembly but is not sufficient. The entire head domain seems to be required for self-assembly. All N-terminal deletion mutants of GFAP share the same phenotype of diffuse cytoplasmic staining when expressed in vimentin-negative SW13 cells. Although co-assembly with vimentin can still be achieved with completely head-less GFAP, preservation of some of the head domain greatly enhanced the efficiency. Our results form the basis for further, more detailed mapping of the essential regions in filament assembly of GFAP and other type III IFs.

InteractionIn Vitroof Type III Intermediate Filament Proteins with Triplex DNA

2002 ◽  
Vol 21 (3) ◽  
pp. 163-188 ◽  
Author(s):  
Guohong Li ◽  
Genrich V. Tolstonog ◽  
Peter Traub
Keyword(s):  
Intermediate Filament ◽  
Triplex Dna ◽  
Intermediate Filament Proteins ◽  
Type Iii
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