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Apolipoprotein B-48 Is the Product of a Messenger RNA with an Organ-Specific In-Frame Stop Codon
Abstract
The primary structure of human apolipoprotein (apo) B-48 has been deduced and shown by a combination of DNA excess hybridization, sequencing of tryptic peptides, cloned complementary DNAs, and intestinal messenger RNAs (mRNAs) to be the product of an intestinal mRNA with an in-frame UAA stop codon resulting from a C to U change in the codon CAA encoding Gln 2153 in apoB-100 mRNA. The carboxyl-terminal Ile 2152 of apoB-48 purified from chylous ascites fluid has apparently been cleaved from the initial translation product, leaving Met 2151 as the new carboxyl-terminus. These data indicate that ∼85% of the intestinal mRNAs terminate within ∼0.1 to 1.0 kilobase downstream from the stop codon. The other ∼15% have lengths similar to hepatic apoB-100 mRNA even though they have the same in-frame stop codon. The organ-specific introduction of a stop codon to a mRNA appears unprecedented and might have implications for cryptic polyadenylation signal recognition and RNA processing.
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Metadata
- Authors
- Chen, S.-H., Habib, G., Yang, C.-Y., Gu, Z.-W., Lee, B. R., Weng, S.-A., Silberman, S. R., Cai, S.-J., Deslypere, J. P., Rosseneu, M., Gotto, A. M., Li, W.-H., & Chan, L.
- Venue
- Science
- Published
- 1987-10-16
- Volume
- 238
- Issue
- 4825
- Pages
- 363-366
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1966933803
- Cited by
- 755
- References
- 0
- FWCI
- 15.98
- Type
- journal article
- Language
- en
- Open access
- closed
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