Specific phosphorylation of SR proteins by mammalian DNA topoisomerase I
Article Abstract:
DNA topoisomerase I acts a protein kinase in the phosphorylation of SR proteins. Researchers purified and analyzed the properties of an enzyme active with SR proteins which proved to be DNA topoisomerase I. The enzyme has no obvious ATP-binding site, though it binds ATP with a dissociation constant of 50 nM. The inhibitors of DNA topoisomerase I, such as camptothecin and its derivatives, block the enzyme activity in the presence of DNA and affect the phosphorylation state of SR proteins. Thus DNA topoisomerase I is a SR protein kinase in the cell.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Crystal structure of the RNA component of bacterial ribonuclease P
Article Abstract:
The crystal structure at 3.85-Angstrom resolution of the RNA component of Thermotoga maritima ribonuclease P is shown. The structure shows the general architecture of the RNA molecule, the inter- and intra-domain interactions, the location of the universally conserved regions, the regions involved in pre-tRNA recognition and the location of the active site.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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Crystal structure of a complex of a type IA DNA topoisomerase with a single-stranded DNA molecule
Article Abstract:
Research is presented concerning the crystal structure of an inactive mutant of Escherichia coli's DNA topoisomerase III within a non-covalent complex. Aspects of the type IA topoisomerase mechanism and rearrangement of DNA are discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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