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Polycistronic expression and RNA-binding specificity of the C. elegans homologue of the spliceosome-associated protein SAP49.
- Source :
-
Journal of biochemistry [J Biochem] 1997 Apr; Vol. 121 (4), pp. 739-45. - Publication Year :
- 1997
-
Abstract
- Splicing of mRNA precursors (pre-mRNAs) occurs in a multimolecular complex, termed spliceosome, which is comprised of pre-mRNA, small nuclear ribonucleoprotein particles (snRNPs), and other protein factors including spliceosome-associated proteins (SAPs). SAP49 is thought to be a subunit of the essential splicing factor SF3b and is involved in U2 snRNP function in mammalian cells. We have isolated a Caenorhabditis elegans cDNA encoding an RNA-binding protein with two RNA recognition motifs (RRMs) which shows extensive similarity to the human SAP49. The primary transcript for this C. elegans SAP49 homologue (cSAP49) seems to contain at least two additional cistrons and can be processed into three different mature mRNAs by trans-splicing. The cSAP49 mRNA, like other mRNAs in the same polycistronic unit, is expressed in most of the developmental stages, consistent with its putative essential function for mRNA splicing. By means of an in vitro RNA selection system, we demonstrate that cSAP49 possesses specific RNA-binding activity which resides in its second RRM.
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites
Cross-Linking Reagents
DNA, Helminth metabolism
Gene Expression Regulation, Developmental
Humans
Molecular Sequence Data
Open Reading Frames
RNA metabolism
RNA Splicing
RNA Splicing Factors
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Selection, Genetic
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Substrate Specificity
Transcription, Genetic
Ultraviolet Rays
Caenorhabditis elegans genetics
Caenorhabditis elegans Proteins
Helminth Proteins genetics
Helminth Proteins metabolism
RNA-Binding Proteins genetics
RNA-Binding Proteins metabolism
Spliceosomes metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-924X
- Volume :
- 121
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 9163526
- Full Text :
- https://doi.org/10.1093/oxfordjournals.jbchem.a021648