NDLI: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure.

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Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure.

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Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lipidot-lifson, Y. Soreq, H. Prody, C. A. Lieman-hurwitz, J. Seidman, S. Gnatt, A. Ginzberg, D. Ben-aziz, R. Lev-lehman, E. Neville, L.
Description	Author Affiliation: Soreq H ( Department of Biological Chemistry, Hebrew University, Jerusalem, Israel.);
Abstract	To study the primary structure of human acetylcholinesterase (AcChoEase; EC 3.1.1.7) and its gene expression and amplification, cDNA libraries from human tissues expressing oocyte-translatable AcChoEase mRNA were constructed and screened with labeled oligodeoxynucleotide probes. Several cDNA clones were isolated that encoded a polypeptide with greater than or equal to 50% identically aligned amino acids to Torpedo AcChoEase and human butyrylcholinesterase (BtChoEase; EC 3.1.1.8). However, these cDNA clones were all truncated within a 300-nucleotide-long G + C-rich region with a predicted pattern of secondary structure having a high Gibbs free energy (-117 kcal/mol) downstream from the expected 5' end of the coding region. Screening of a genomic DNA library revealed the missing 5' domain. When ligated to the cDNA and constructed into a transcription vector, this sequence encoded a synthetic mRNA translated in microinjected oocytes into catalytically active AcChoEase with marked preference for acetylthiocholine over butyrylthiocholine as a substrate, susceptibility to inhibition by the AcChoEase inhibitor BW284C51, and resistance to the BtChoEase inhibitor tetraisopropylpyrophosphoramide. Blot hybridization of genomic DNA from different individuals carrying amplified AcChoEase genes revealed variable intensities and restriction patterns with probes from the regions upstream and downstream from the predicted G + C-rich structure. Thus, the human AcChoEase gene includes a putative G + C-rich attenuator domain and is subject to structural alterations in cases of AcChoEase gene amplification.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetylcholinesterase Genetics Metabolism Amino Acid Sequence Animals Cloning, Molecular Cytosine Gene Amplification Gene Library Guanine Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Oligonucleotide Probes Oocytes Enzymology Protein Biosynthesis RNA, Messenger Restriction Mapping Sequence Homology, Nucleic Acid Torpedo Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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