atSRp30, one of two SF2/ASF-like proteins from Arabidopsis thaliana, regulates splicing of specific plant genes

Article Abstract:

A plant protein which crossreacts with antibodies to human serine/argininine (SR) proteins has been isolated and partially sequenced. SR proteins are nuclear phosphoproteins with a Ser/Arg-rich domain that is characteristic and up to two RNA recognition motifs. The proteins are much conserved in plants and animals and have important roles in alternative splicing regulation and spliceosome assembly. The sequence of the corresponding cDNA and genomic clones from Arabidopsis thaliana found a protein, atSRp30. The protein was very similar to the human SR protein SF2/ASG and to atSRp34/SR1, already identified and an SR protein. This indicates that plants have two SF2/ASF-like proteins. Analyses show that it is probable that atSRp30, one of two SF2/ASF-like proteins from Arabidopsis, acts as a regulator for splicing of specific plant genes.

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Identification of eight proteins that cross-link to pre-mRNA in the yeast commitment complex

Article Abstract:

Eight proteins that cross-link to pre-mRNA in the yeast commitment complex have been identified in a study in which 4-thiouridine-substituted 5' spice site-containing RNAs were used as substrates. The proteins were in the exon domain, the downstream intron and the six nucleotides of the 5' ss region, three domains. The 5' splice site region and the area around it appear to have many protein contacts in the commitment complex. It seems some of them make valuable contributions to stability or formation of the U1 snRNP-pre-mRNA complex.

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Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta-tropomyosin gene

Article Abstract:

The activating effect of a six-nucleotide mutation at the 5' end of exon 7, does not come from creation of an exonic splicing enhancer (ESE) or from disrupting a putative secondary structure. The sequence in exon 7 behaves as a genuine exonic splicing silencer (ESS) bound specifically by a trans-acting factor. Binding hnRNP H to an exonic splicing silencer is a part of the regulation of alternative splicing of the rat beta-tropomyosin gene.

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