Donate Help Contact The AHA Sign In Home
American Heart Association
Arteriosclerosis, Thrombosis, and Vascular Biology
Search: search_blue_button Advanced Search
« Previous Article | Table of Contents | Next Article »
Arteriosclerosis, Thrombosis, and Vascular Biology. 1992;12:172-179

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Garcia, Z. C.
Right arrow Articles by Innerarity, T. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Garcia, Z. C.
Right arrow Articles by Innerarity, T. L.

Arteriosclerosis and Thrombosis, Vol 12, 172-179, Copyright © 1992 by American Heart Association

ARTICLES

Characterization of apolipoprotein B mRNA editing from rabbit intestine

ZC Garcia, KS Poksay, K Bostrom, DF Johnson, ME Balestra, I Shechter and TL Innerarity
Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.

Apolipoprotein (apo) B-48 is generated by a unique physiological process. Cytidine 6,666 of the apo B primary transcript is posttranscriptionally converted to a uridine by an RNA editing mechanism that transforms the codon for glutamine 2,153 to a termination codon. The editing reaction can be duplicated in a cell- free extract. In this study, the apo B-48 mRNA editing activity derived from partially purified extracts of rabbit enterocytes was characterized. The optimum conditions for the editing reaction were determined to be a salt concentration of 0.125-0.150 M NaCl or KCl, a pH of 8-8.5, and a temperature of 30 degrees C. The reaction rate was linear up to 45 minutes and was proportional to the editing extract concentration. No metal ion cofactors, DNA or RNA cofactors, or energy requirements were identified. At optimum conditions, the reaction followed Michaelis-Menten kinetics, with a Km of 0.4 nM for the rabbit RNA substrate. In addition, the reaction rate was enhanced by the addition of 25 micrograms/ml heparin or 40% glycerol. The characteristics of the editing reaction suggest that it is catalyzed by a nucleotide sequence-specific cytidine deaminase that is either a single enzyme or a multimeric protein.


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
G. S. C. Dance, P. Beemiller, Y. Yang, D. V. Mater, I. S. Mian, and H. C. Smith
Identification of the yeast cytidine deaminase CDD1 as an orphan C{->}U RNA editase
Nucleic Acids Res., April 15, 2001; 29(8): 1772 - 1780.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Mehta, M. T. Kinter, N. E. Sherman, and D. M. Driscoll
Molecular Cloning of Apobec-1 Complementation Factor, a Novel RNA-Binding Protein Involved in the Editing of Apolipoprotein B mRNA
Mol. Cell. Biol., March 1, 2000; 20(5): 1846 - 1854.
[Abstract] [Full Text]

Home page
 Nucleic Acids ResHome page
G. S. C. Dance, M. P. Sowden, Y. Yang, and H. C. Smith
APOBEC-1 dependent cytidine to uridine editing of apolipoprotein B RNA in yeast
Nucleic Acids Res., January 15, 2000; 28(2): 424 - 429.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Hersberger, S. Patarroyo-White, K. S. Arnold, and T. L. Innerarity
Phylogenetic Analysis of the Apolipoprotein B mRNA-editing Region. EVIDENCE FOR A SECONDARY STRUCTURE BETWEEN THE MOORING SEQUENCE AND THE 3' EFFICIENCY ELEMENT
J. Biol. Chem., December 3, 1999; 274(49): 34590 - 34597.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Mehta and D. M. Driscoll
A Sequence-Specific RNA-Binding Protein Complements Apobec-1 To Edit Apolipoprotein B mRNA
Mol. Cell. Biol., August 1, 1998; 18(8): 4426 - 4432.
[Abstract] [Full Text]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
J. Greeve, D. Axelos, S. Welker, M. Schipper, and H. Greten
Distinct Promoters Induce APOBEC-1 Expression in Rat Liver and Intestine
Arterioscler Thromb Vasc Biol, July 1, 1998; 18(7): 1079 - 1092.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Hersberger and T. L. Innerarity
Two Efficiency Elements Flanking the Editing Site of Cytidine 6666 in the Apolipoprotein B mRNA Support Mooring-dependent Editing
J. Biol. Chem., April 17, 1998; 273(16): 9435 - 9442.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Mehta, S. Banerjee, and D. M. Driscoll
Apobec-1 Interacts with a 65-kDa Complementing Protein to Edit Apolipoprotein-B mRNA in Vitro
J. Biol. Chem., November 8, 1996; 271(45): 28294 - 28299.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Anant, A. J. MacGinnitie, and N. O. Davidson
apobec-1, the Catalytic Subunit of the Mammalian Apolipoprotein B mRNA Editing Enzyme, Is a Novel RNA-binding Protein
J. Biol. Chem., June 16, 1995; 270(24): 14762 - 14767.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
B Teng, C. Burant, and N. Davidson
Molecular cloning of an apolipoprotein B messenger RNA editing protein
Science, June 18, 1993; 260(5115): 1816 - 1819.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
H. Lellek, R. Kirsten, I. Diehl, F. Apostel, F. Buck, and J. Greeve
Purification and Molecular Cloning of a Novel Essential Component of the Apolipoprotein B mRNA Editing Enzyme-Complex
J. Biol. Chem., June 23, 2000; 275(26): 19848 - 19856.
[Abstract] [Full Text] [PDF]


ATVB Home | Subscriptions | Archives | Feedback | Authors | Help | AHA Journals Home | Search
Copyright © 1992 American Heart Association, Inc. All rights reserved. Unauthorized use prohibited.