A single amino acid substitution in the enzyme 5-enolpyruvylshikimate-3-phosphate synthase confers resistance to the herbicide glyphosate.
作者： D M Stalker , W R Hiatt , L Comai
DOI: 10.1016/S0021-9258(18)89130-X
关键词: Molecular biology 、 Mutant 、 EPSP synthase 、 Aroa 、 Subcloning 、 Gene 、 Biology 、 Nucleic acid sequence 、 Amino acid 、 Biochemistry 、 Wild type
摘要: The enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.19), encoded by the aroA locus, is a target site of glyphosate inhibition in bacteria. A glyphosate-resistant allele has been cloned Escherichia coli from mutagenized strain Salmonella typhimurium. Subcloning this mutant shows gene to reside on 1.3-kilobase segment S. typhimurium DNA. Nucleotide sequence analysis indicates protein-coding region 427 amino acids length. Comparison and wild type sequences reveals single base pair change resulting Pro Ser acid substitution at 101st codon protein. hybrid fusion between was constructed. 5-Enolpyruvylshikimate-3-phosphate prepared E. cells harboring construct. phenotype shown be associated with described above.
sci-hub.st 参考文章(23)
S G Rogers, L A Brand, S B Holder, E S Sharps, M J Brackin, Amplification of the aroA gene from Escherichia coli results in tolerance to the herbicide glyphosate. Applied and Environmental Microbiology. ,vol. 46, pp. 37- 43 ,(1983) , 10.1128/AEM.46.1.37-43.1983
Michael Kahn, Roberto Kolter, Christopher Thomas, David Figurski, Richard Meyer, Eric Remaut, Donald R. Helinski, [17] Plasmid cloning vehicles derived from plasmids ColE1, F, R6K, and RK2 Methods in Enzymology. ,vol. 68, pp. 268- 280 ,(1979) , 10.1016/0076-6879(79)68019-9
Brian P. Nichols, Magda van Cleemput, Charles Yanofsky, Nucleotide sequence of Escherichia coli trpE: Anthranilate synthetase component I contains no tryptophan residues Journal of Molecular Biology. ,vol. 146, pp. 45- 54 ,(1981) , 10.1016/0022-2836(81)90365-X
E. Gollub, H. Zalkin, D.B. Sprinson, Correlation of Genes and Enzymes, and Studies on Regulation of the Aromatic Pathway in Salmonella Journal of Biological Chemistry. ,vol. 242, pp. 5323- 5328 ,(1967) , 10.1016/S0021-9258(18)99431-7
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
Kenneth Duncan, Ann Lewendon, John R. Coggins, The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain ofEscherichia coli FEBS Letters. ,vol. 165, pp. 121- 127 ,(1984) , 10.1016/0014-5793(84)80027-7
Theodore Friedmann, Daniel M. Brown, Base-specific reactions useful for DNA sequencing: methylene blue – sensitized photooxidation of guanine and osmium tetraoxide modification of thymine Nucleic Acids Research. ,vol. 5, pp. 615- 622 ,(1978) , 10.1093/NAR/5.2.615
Kenneth Duncan, Ann Lewendon, John R. Coggins, The complete amino acid sequence of Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase FEBS Letters. ,vol. 170, pp. 59- 63 ,(1984) , 10.1016/0014-5793(84)81368-X
A. M. Maxam, W. Gilbert, A new method for sequencing DNA Proceedings of the National Academy of Sciences of the United States of America. ,vol. 74, pp. 560- 564 ,(1977) , 10.1073/PNAS.74.2.560
David L. Anton, Lizbeth Hedstrom, Susan M. Fish, Robert H. Abeles, Mechanism of enolpyruvylshikimate-3-phosphate synthase exchange of phosphoenolpyruvate with solvent protons Biochemistry. ,vol. 22, pp. 5903- 5908 ,(1983) , 10.1021/BI00294A033