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Alternative splicing generates two different mRNA species for rat link protein
1Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research, Bethesda, Maryland 20892.
The Journal of Biological Chemistry
|May 5, 1988
Summary
Researchers identified two forms of rat link protein (link 45 and link 39) through cDNA cloning. Link 39 represents the primary chondrosarcoma form, while link 45 includes an additional exon.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Previous isolation of a cDNA clone encoding the carboxyl-terminal portion of rat link protein.
- The current study focuses on isolating cDNA clones for the remaining part of the protein.
Purpose of the Study:
- To isolate and characterize cDNA clones encoding the full-length rat link protein.
- To investigate the structural variations and genomic organization of rat link protein.
Main Methods:
- cDNA cloning and sequence analysis to identify different forms of link protein.
- Genomic cloning and sequencing to determine exon-intron structure.
- Northern blotting to analyze link protein transcript sizes and prevalence.
Main Results:
- Two classes of cDNA clones were identified, differing by a 159-base pair internal segment encoding 53 amino acids, resulting in link 45 and link 39.
- Genomic analysis revealed this segment corresponds to a single exon.
- Link 39 (Mr = 38,570) represents the predominant form in chondrosarcoma, while link 45 (Mr = 44,779) is less prevalent.
- Both forms' transcripts hybridized to similar size classes, indicating alternative splicing.
Conclusions:
- Rat link protein exhibits alternative splicing, generating at least two forms (link 45 and link 39).
- The predominant form in chondrosarcoma is link 39.
- The structural similarity of link 45 to a larger form (LP1) in other species is coincidental.