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Interaction between the N-terminal domain of human DNA topoisomerase I and the arginine-serine domain of its substrate determines phosphorylation of SF2/ASF splicing factor.

Human DNA topoisomerase I, known for its DNA-relaxing activity, is possibly one of the kinases phosphorylating members of the SR protein family of splicing factors, in vivo. Little is known about the mechanism of action of this novel kinase. Using the prototypical SR protein SF2/ASF (SRp30a) as mode...

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Bibliografiske detaljer
Udgivet i:Nucleic Acids Res
Principais autores: Labourier, E, Rossi, F, Gallouzi, I E, Allemand, E, Divita, G, Tazi, J
Format: Artigo
Sprog:Inglês
Udgivet: Oxford University Press 1998
Fag:
Online adgang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC147637/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9611241/
https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/26.12.2955
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