NDLI: Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

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Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

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Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Scappino, L. A. Ward, E. Dimaio, J. Haselkorn, R. Gornicki, P. Podkowinski, J.
Description	Author Affiliation: Gornicki P ( Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.);
Abstract	cDNA fragments encoding part of wheat (Triticum aestivum) acetyl-CoA carboxylase (ACC; EC 6.4.1.2) were cloned by PCR using primers based on the alignment of several biotin-dependent carboxylases. A set of overlapping clones encoding the entire wheat ACC was then isolated by using these fragments as probes. The cDNA sequence contains a 2257-amino acid reading frame encoding a 251-kDa polypeptide. The amino acid sequence of the most highly conserved domain, corresponding to the biotin carboxylases of prokaryotes, is 52-55% identical to ACC of yeast, rat, and diatom. Identity with the available C-terminal amino acid sequence of maize ACC is 66%. The biotin attachment site has the typical eukaryotic EVMKM sequence. The cDNA does not encode an obvious chloroplast targeting sequence. Various cDNA fragments hybridize in Northern blots to a 7.9-kb mRNA. Southern analysis with cDNA probes revealed multiple hybridizing fragments in hexaploid wheat DNA. Some of the wheat cDNA probes also hybridize with ACC-specific DNA from other plants, indicating significant conservation among plant ACCs.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyl-CoA Carboxylase Genetics Triticum Amino Acid Sequence Animals DNA Molecular Sequence Data Polymerase Chain Reaction Protein Conformation Sequence Homology, Amino Acid Enzymology Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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