An amino acid sequence motif sufficient for subnuclear localization of an arginine/serine-rich splicing factor.

AUTOR(ES)

Hedley, M L

RESUMO

We have identified an amino acid sequence in the Drosophila Transformer (Tra) protein that is capable of directing a heterologous protein to nuclear speckles, regions of the nucleus previously shown to contain high concentrations of spliceosomal small nuclear RNAs and splicing factors. This sequence contains a nucleoplasmin-like bipartite nuclear localization signal (NLS) and a repeating arginine/serine (RS) dipeptide sequence adjacent to a short stretch of basic amino acids. Sequence comparisons from a number of other splicing factors that colocalize to nuclear speckles reveal the presence of one or more copies of this motif. We propose a two-step subnuclear localization mechanism for splicing factors. The first step is transport across the nuclear envelope via the nucleoplasmin-like NLS, while the second step is association with components in the speckled domain via the RS dipeptide sequence.

Documentos Relacionados

• Characterization of a novel arginine/serine-rich splicing factor in Arabidopsis.
• Serine–arginine (SR)-rich splicing factors have an exon-independent function in pre-mRNA splicing
• Arginine/serine repeats are sufficient to constitute a splicing activation domain
• Identification of a plant serine-arginine-rich protein similar to the mammalian splicing factor SF2/ASF.
• Identification and Characterization of a Novel Serine-Arginine-Rich Splicing Regulatory Protein