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The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteins
B Funke1, B Zuleger, R Benavente
1Institut für Virologie und Immunbiologie der Universität Würzburg, Germany.
Nucleic Acids Research
|October 1, 1996
Summary
Murine poly(C)-binding protein (mCBP) splice variants were identified, differing in two variable regions. These variants, interacting with several proteins, suggest a role for mCBP in RNA metabolism.
Area of Science:
- Molecular Biology
- RNA Biology
- Protein Interactions
Background:
- Murine poly(C)-binding protein (mCBP) is homologous to hnRNP-K, classifying it as a K-homology (KH) protein.
- Previous studies established mCBP's homology to hnRNP-K, placing it within the KH protein family.
Purpose of the Study:
- To isolate and characterize cDNA splice variants of mCBP.
- To investigate the genomic basis for alternative splicing in mCBP.
- To identify proteins interacting with mCBP and elucidate its cellular function.
Main Methods:
- cDNA isolation and characterization of splice variants.
- Genomic clone analysis to model alternative splicing.
- Yeast two-hybrid system for protein-protein interaction studies.
- In vivo validation of protein interactions.
Main Results:
- Isolated mCBP cDNA splice variants differing by two variable regions (93 bp and 39 bp).
- Proposed a model for alternative splicing generating the second variable region.
- Identified five interacting proteins: msy-1, y-box-binding protein, hnRNP-L, filamin, and splicing factor 9G8.
- Confirmed in vivo interaction between mCBP and splicing factor 9G8.
- Ubiquitous mCBP mRNA expression with nuclear localization (excluding nucleoli).
Conclusions:
- mCBP exhibits alternative splicing, generating distinct protein variants.
- mCBP interacts with multiple proteins involved in RNA processing.
- These findings strongly suggest a functional role for mCBP in RNA metabolism.