Members of the hnRNP H protein family bind the consensus motif DGGGD and activate splicing of an HIV-1 tat-derived substrate by promoting ATP-dependent spliceosomal complex formation.
Members of the hnRNP H protein family activate splicing of an HIV-1 substrate by promoting the formation of ATP-dependent spliceosomal complexes.
In this study we analyzed members of the heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family to determine their RNA binding specificities and roles in splicing regulation. Our data indicate that hnRNPs H, H', F, 2H9, and GRSF-1 bind the consensus motif DGGGD (where D is U, G, or A) and aggregate in a multimeric complex. We analyzed the role of these proteins in the splicing of a substrate derived from the HIV-1 tat gene and have shown that hnRNP H family members are required for efficient splicing of this substrate. The hnRNP H protein family members activated splicing of the viral substrate by promoting the formation of ATP-dependent spliceosomal complexes. Mutational analysis of six consensus motifs present within the intron of the substrate indicated that only one of these motifs acts as an intronic splicing enhancer.
Schaub et al. (Sat,) conducted a other in HIV-1. hnRNP H family proteins was evaluated on Splicing of a substrate derived from the HIV-1 tat gene. Members of the hnRNP H protein family bind the consensus motif DGGGD and activate splicing of an HIV-1 tat-derived substrate by promoting ATP-dependent spliceosomal complex formation.
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