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. 1974 Apr;118(1):187–191. doi: 10.1128/jb.118.1.187-191.1974

Amino-Terminal Sequence of the Tryptophan Synthetase α Chain of Bacillus subtilis

Shoei-Lung Li 1,2, Sallie O Hoch 1,2
PMCID: PMC246656  PMID: 4206869

Abstract

The sequence of the 46 NH2-terminal residues of the tryptophan synthetase α chain of Bacillus subtilis was determined and compared with the corresponding sequences of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium, Aerobacter aerogenes, Serratia marcescens, and Pseudomonas putida. A deletion of six residues was found at the NH2-terminal end of the α chain of B. subtilis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Crawford I. P., Yanofsky C. Pseudomonas putida tryptophan synthetase: partial sequence of the subunit. J Bacteriol. 1971 Oct;108(1):248–253. doi: 10.1128/jb.108.1.248-253.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  3. Guest J. R., Drapeau G. R., Carlton B. C., Yanofsky C. The amino acid sequence of the A protein (alpha subunit) of the tryptophan synthetase of Escherichia coli. J Biol Chem. 1967 Nov 25;242(22):5442–5446. [PubMed] [Google Scholar]
  4. Hoch S. O. Tryptophan synthetase from Bacillus subtilis. Purification and characterization of the component. J Biol Chem. 1973 May 10;248(9):2999–3003. [PubMed] [Google Scholar]
  5. Li S. L., Denney R. M., Yanofsky C. Nucleotide sequence divergence in the -chain-structural genes of tryptophan synthetase from Escherichia coli, Salmonella typhimurium, and Aerobacter aerogenes. Proc Natl Acad Sci U S A. 1973 Apr;70(4):1112–1116. doi: 10.1073/pnas.70.4.1112. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Li S. L., Drapeau G. R., Yanofsky C. Amino terminal sequence of the tryptophan synthetase alpha chain of Serratia marcescens. J Bacteriol. 1973 Mar;113(3):1507–1508. doi: 10.1128/jb.113.3.1507-1508.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Li S. L., Yanofsky C. Amino acid sequence studies with the tryptophan synthetase chain of Aerobacter aerogenes. J Biol Chem. 1973 Mar 10;248(5):1837–1843. [PubMed] [Google Scholar]
  8. Li S. L., Yanofsky C. Amino acid sequence studies with the tryptophan synthetase chain of Salmonella typhimurium. J Biol Chem. 1973 Mar 10;248(5):1830–1836. [PubMed] [Google Scholar]
  9. Li S. L., Yanofsky C. Amino acid sequences of fifty residues from the amino termini of the tryptophan synthetase chains of several enterobacteria. J Biol Chem. 1972 Feb 25;247(4):1031–1037. [PubMed] [Google Scholar]
  10. Pisano J. J., Bronzert T. J. Analysis of amino acid phenylthiohydantoins by gas chromatography. J Biol Chem. 1969 Oct 25;244(20):5597–5607. [PubMed] [Google Scholar]
  11. Prakash L., Sherman F. Mutagenic specificity: reversion of iso-1-cytochrome c mutants of yeast. J Mol Biol. 1973 Sep 5;79(1):65–82. doi: 10.1016/0022-2836(73)90270-2. [DOI] [PubMed] [Google Scholar]
  12. Smithies O., Gibson D., Fanning E. M., Goodfliesh R. M., Gilman J. G., Ballantyne D. L. Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac. Biochemistry. 1971 Dec 21;10(26):4912–4921. doi: 10.1021/bi00802a013. [DOI] [PubMed] [Google Scholar]
  13. YANOFSKY C., HORN V., THORPE D. PROTEIN STRUCTURE RELATIONSHIPS REVEALED BY MUTATIONAL ANALYSIS. Science. 1964 Dec 18;146(3651):1593–1594. doi: 10.1126/science.146.3651.1593. [DOI] [PubMed] [Google Scholar]
  14. Yanofsky C., Horn V. Tryptophan synthetase chain positions affected by mutations near the ends of the genetic map of trpA of Escherichia coli. J Biol Chem. 1972 Jul 25;247(14):4494–4498. [PubMed] [Google Scholar]

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