Association of the adenovirus DNA-binding protein with RNA both in vitro and in vivo.

AUTOR(ES)

Cleghon, V G

RESUMO

The multifunctional DNA-binding protein (DBP) encoded by human adenovirus binds RNA. The association of purified DBP with RNA in vitro was demonstrated by using either a gel filtration or a filter binding assay. This association is sensitive to ionic strength and exhibits no apparent sequence specificity. DBP also interacts with RNA in vivo; it can be crosslinked to polyadenylylated RNA by UV-irradiation of intact cells during the late phase of adenovirus infections. The 46-kDa carboxyl-terminal domain of DBP binds RNA in vitro and was found to be associated with polyadenylylated RNA in vivo. This is the same domain that interacts with DNA. However, the differences in sensitivity of DBP to trypsin when bound to RNA versus DNA suggest that RNA and DNA either bind at different sites within this domain or induce different conformational changes within the protein.

Documentos Relacionados

• Adenovirus-specific DNA-binding protein inhibits the hydrolysis of DNA by DNase in vitro.
• Role of the Adenovirus DNA-Binding Protein in In Vitro Adeno-Associated Virus DNA Replication
• Functional specificity of the homeodomain protein fushi tarazu: the role of DNA-binding specificity in vivo.
• The adenovirus type 2 DNA-binding protein interacts with the major late promoter attenuated RNA.
• Helix-destabilizing properties of the adenovirus DNA-binding protein.