Apolipoprotein B-48 is the Product of a Messenger RNA with an Organ-Specific In-Frame Stop Codon

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 r...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) Vol. 238; no. 4825; pp. 363 - 366
Main Authors: Chen, San-Hwan, Habib, Geetha, Yang, Chao-Yuh, Gu, Zi-Wei, Lee, Bo Rong, Weng, Shi-ai, Silberman, Steven R., Cai, Sheng-Jian, Deslypere, J. P., Rosseneu, Maryvonne, Gotto, Antonio M., Li, Wen-Hsiung, Chan, Lawrence
Format: Journal Article
Language:English
Published: Washington, DC The American Association for the Advancement of Science 16-10-1987
American Association for the Advancement of Science
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 $\sim $85% of the intestinal mRNAs terminate within $\sim $0.1 to 1.0 kilobase downstream from the stop codon. The other $\sim $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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Article-2
ObjectType-Feature-1
ISSN:0036-8075
1095-9203
DOI:10.1126/science.3659919