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  • Title: Different species of messenger RNA encode receptor and secretory IgM mu chains differing at their carboxy termini.
    Author: Singer PA, Singer HH, Williamson AR.
    Journal: Nature; 1980 May 29; 285(5763):294-300. PubMed ID: 6769053.
    Abstract:
    Biosynthetic studies in the presence of an inhibitor of glycosylation indicate that individual human lymphoma-derived cell lines can synthesize both membrne receptor and presumptive secretory forms of IgM mu chains. The receptor form has a larger polypeptide chain than the secretory form and possesses a different C-terminus, but similar N-terminus, consistent with the presence of a C-terminal hydrophobic "tail" for integral membrane binding. Messenger RNA isolated from these cells directs the synthesis of both forms of mu chains in a wheat germ translation system, indicating the presence of independent mRNAs for each form. It is proposed that the synthetic pathways for receptor and secretory IgM diverge at the post-transcriptional level, possibly by differential RNA splicing to give mRNA molecules with or without a translatable "tail" segment.
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