Isolation of SDS-stable complexes of the intermediate filament protein vimentin with repetitive, mobile, nuclear matrix attachment region, and mitochondrial DNA sequence elements from cultured mouse and human fibroblasts.

Details

Serval ID
serval:BIB_B84FD1D5443E
Type
Article: article from journal or magazin.
Collection
Publications
Title
Isolation of SDS-stable complexes of the intermediate filament protein vimentin with repetitive, mobile, nuclear matrix attachment region, and mitochondrial DNA sequence elements from cultured mouse and human fibroblasts.
Journal
DNA and cell biology
Author(s)
Tolstonog G.V., Mothes E., Shoeman R.L., Traub P.
ISSN
1044-5498 (Print)
ISSN-L
1044-5498
Publication state
Published
Issued date
09/2001
Peer-reviewed
Oui
Volume
20
Number
9
Pages
531-554
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
Crosslinkage of vimentin to DNA in mouse L929 cells by formaldehyde and isolation of SDS-stable DNA-vimentin complexes from normal L929 cells and mouse and human embryo fibroblasts indicated close spatial relations between these components in the intact cell. The adducts, obtained by immunoprecipitation with anti-vimentin antibody, contained substantial quantities, not only of repetitive and mobile sequence elements such as centromeric satellite DNA, telomere DNA, microsatellites and minisatellites, long and short interspersed nucleotide elements, and retroposons, but also of mitochondrial (mt) DNA. Because the SDS-stable complexes could be isolated with distinctly higher yields from oxidatively stressed, senescent fibroblasts and were dissociated by boiling, they possibly arose from accidental condensation reactions mediated by unsaturated and dialdehydes, products of free radical-induced lipid peroxidation. They can therefore be considered vestiges of a general interaction of vimentin with cellular DNA. The sequence patterns of their DNA fragments were similar to those of extrachromosomal circular and linear DNA, including retroviral elements, markers and enhancers of genomic instability that also occur in the cytoplasm and are able to transport vimentin into the nucleus. Many of the fragments were also remarkably similar to AT-rich nuclear matrix attachment regions (MARs) in that they contained, in addition to various mobile elements, a palette of typical MAR motifs. With its tendency to multimerize and to interact with single-stranded and supercoiled DNA, vimentin thus behaves like a nuclear matrix protein and may as such participate in a variety of nuclear matrix-associated processes such as replication, recombination, repair, and transcription of DNA. These activities seem to be extendible to the mitochondrial compartment, as vimentin was also crosslinked to mtDNA, preferentially to its D-loop and hypervariable main control region. These sites are prone to point and deletion mutations and, like nuclear MARs, are associated with the cyto-karyomatrix. Moreover, as a developmentally regulated and tissue-specific cyto-karyomatrix protein, vimentin may contribute to the organization of chromatin, including centromeric and telomeric heterochromatin at the nuclear periphery, with all its consequences for genomic activities during embryogenesis and in adulthood of vertebrates. However, because of its high affinity for hypervariable, recombinogenic DNA sequences, vimentin is proposed to play a major role in both the preservation and the evolution of the nuclear and mitochondrial genome.
Keywords
Animals, Base Sequence, Cells, Cultured, Cross-Linking Reagents, DNA/genetics, DNA/metabolism, DNA, Complementary/analysis, DNA, Complementary/genetics, DNA, Mitochondrial/genetics, DNA, Mitochondrial/metabolism, Embryo, Mammalian, Fibroblasts, Humans, Interspersed Repetitive Sequences, Mice, Molecular Sequence Data, Nuclear Matrix/metabolism, Protein Binding, Sodium Dodecyl Sulfate, Vimentin/genetics, Vimentin/metabolism
Pubmed
Web of science
Create date
15/12/2017 16:26
Last modification date
14/01/2020 6:26
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