Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences
- 1 October 1988
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 177 (1) , 153-158
- https://doi.org/10.1111/j.1432-1033.1988.tb14356.x
Abstract
The structural gene of pyruvate formate-lyase (pfl) and that of pyruvate-formate-lyase-activating enzyme were shown to be adjacent on the chromosomal map of Escherichia coli. DNA sequencing was performed along a stretch of 3592 nucleotides to obtain the amino acid sequences of both proteins. The derived primary structures (759 and 245 residues) were confirmed by partial structure analyses on the purified proteins. The open reading frames are separated by a 194-nucleotide stretch, and their flanking regions include signal elements that are compatible with separate control of protein synthesis from the two genes.Keywords
This publication has 13 references indexed in Scilit:
- [57] Sequencing end-labeled DNA with base-specific chemical cleavagesPublished by Elsevier ,2004
- The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic libraryCell, 1987
- An Improved Gas-Phase Sequenator Including On-line Identification of PTH Amino AcidsPublished by Springer Nature ,1986
- Post-translational activation introduces a free radical into pyruvate formate-lyase.Proceedings of the National Academy of Sciences, 1984
- Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: Isolation and structural propertiesArchives of Biochemistry and Biophysics, 1984
- [7] Amino acid analysis in the picomole range by precolumn derivatization and high-performance liquid chromatographyPublished by Elsevier ,1983
- Expression of pyruvate formate-lyase of Escherichia coli from the cloned structural geneArchiv für Mikrobiologie, 1982
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- Use of carboxypeptidase Y for carboxy-terminal sequence determination in proteinsCarlsberg Research Communications, 1977
- Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric ProteinsProceedings of the National Academy of Sciences, 1970