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Bidirectional DNA unwinding by a ternary complex of T antigen, nucleolin and topoisomerase I.
- Source :
-
EMBO reports [EMBO Rep] 2003 Mar; Vol. 4 (3), pp. 263-8. - Publication Year :
- 2003
-
Abstract
- The simian virus 40 large tumour-antigen (T antigen) DNA helicase is a hexameric structure; it has been proposed that, in viral DNA replication, two of these hexamers are combined to form a bipartite holoenzyme that acts concurrently at both forks of a replication bubble. In a search for structural components of this helicase complex, we have identified nucleolin as a specific binding protein for the T-antigen hexamer. We show that nucleolin, in co-operation with human topoisomerase I, mediates the cohesion of the T-antigen helicase holoenzyme during plasmid unwinding. Our results provide biochemical evidence for a direct role of nucleolin in DNA replication, in addition to its known function in ribosome biogenesis. The data presented here suggest that nucleolin enables the formation of a functional 'helicase-swivelase' complex at the replication fork.
- Subjects :
- Amino Acid Sequence
Animals
Antigens, Viral, Tumor chemistry
Antigens, Viral, Tumor genetics
COS Cells
Cell Line
Chlorocebus aethiops
DNA chemistry
DNA ultrastructure
HeLa Cells
Humans
Molecular Sequence Data
Nuclear Proteins metabolism
Peptide Fragments immunology
Recombinant Proteins metabolism
Simian virus 40 immunology
Spodoptera
Transfection
Nucleolin
Antigens, Viral, Tumor metabolism
DNA genetics
DNA Helicases metabolism
DNA Topoisomerases, Type I metabolism
Phosphoproteins metabolism
RNA-Binding Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1469-221X
- Volume :
- 4
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- EMBO reports
- Publication Type :
- Academic Journal
- Accession number :
- 12634843
- Full Text :
- https://doi.org/10.1038/sj.embor.embor770