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Identification and characterization of RED120: A conserved PWI domain protein with links to splicing and 3′-end formation
- Source :
- FEBS Letters. (16):3087-3097
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
Abstract
- Precursor (pre)-mRNA splicing can impact the efficiency of coupled steps in gene expression. SRm160 (SR-related nuclear matrix protein of 160kDa), is a splicing coactivator that also functions as a 3′-end cleavage-stimulatory factor. Here, we have identified an evolutionary-conserved SRm160-interacting protein, referred to as hRED120 (for human Arg/Glu/Asp-rich protein of 120kDa). hRED120 contains a conventional RNA recognition motif and, like SRm160, a PWI nucleic acid binding domain, suggesting that it has the potential to bridge different RNP complexes. Also, similar to SRm160, hRED120 associates with snRNP components, and remains associated with mRNA after splicing. Simultaneous suppression in Caenorhabditis elegans of the ortholog of hRED120 with the orthologs of splicing and 3′-end processing factors results in aberrant growth or developmental defects. These results suggest that RED120 may function to couple splicing with mRNA 3′-end formation.
- Subjects :
- RNA Splicing
Molecular Sequence Data
Biophysics
Exonic splicing enhancer
RNA-binding protein
snRNPs
Biology
Splicing
Biochemistry
Splicing factor
SR protein
Nuclear Matrix-Associated Proteins
Structural Biology
Protein splicing
Genetics
RNA Precursors
3′-End processing
Animals
Humans
snRNP
Amino Acid Sequence
RNA, Messenger
Cloning, Molecular
Caenorhabditis elegans
Molecular Biology
Conserved Sequence
Phylogeny
Cell Nucleus
Sequence Homology, Amino Acid
Alternative splicing
Nuclear Proteins
RNA-Binding Proteins
Antigens, Nuclear
SRm160
Cell Biology
Cell biology
Protein Structure, Tertiary
RNAi
RNA splicing
RNA 3' End Processing
HeLa Cells
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 16
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....564310201aa8276f34d35897e03bb7d3
- Full Text :
- https://doi.org/10.1016/j.febslet.2007.05.066