Alternative splicing of human T-cell-specific MAL mRNA and its correlation with the exon/intron organization of the gene.
Sequence analysis of the T-cell-specific MAL gene revealed four exons, each encoding a hydrophobic, presumably membrane-associated, segment and its adjacent hydrophilic sequence. Amplification by the polymerase chain reaction of cDNA from different T-cell samples indicated the existence of four different forms of MAL mRNA, termed MAL-a, -b, -c, and -d, that arise from differential usage of exons II and/or III. As the three introns were located between complete codons, the reading frame was maintained in all the transcripts. A model resembling the structures postulated for different proteolipid proteins is proposed for the protein encoded by each alternative mRNA species.
Rancaño
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Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Spain.
Rubio
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Alonso
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D017398:Alternative Splicing; D001483:Base Sequence; D002460:Cell Line; D017931:DNA Primers; D005091:Exons; D006801:Humans; D007438:Introns; D026901:Membrane Transport Proteins; D008969:Molecular Sequence Data; D009185:Myelin Proteins; D062806:Myelin and Lymphocyte-Associated Proteolipid Proteins; D016133:Polymerase Chain Reaction; D014176:Protein Biosynthesis; D011506:Proteins / Q000235:genetics; D011510:Proteolipids; D012333:RNA, Messenger / Q000378:metabolism*; D015183:Restriction Mapping; D013601:T-Lymphocytes / Q000378:metabolism*; D014158:Transcription, Genetic
D017931:DNA Primers; C569026:MAL protein, human; D026901:Membrane Transport Proteins; D009185:Myelin Proteins; D062806:Myelin and Lymphocyte-Associated Proteolipid Proteins; D011506:Proteins; D011510:Proteolipids; D012333:RNA, Messenger