Crossref journal-article
American Society for Microbiology
Journal of Bacteriology (235)
Abstract

Construction and characterization of double mutants altered in the structural gene of the tryptophan synthetase alpha chain of Escherichia coli revealed interactions between amino acid residues at positions 22 and 211. These interactions are specific for the particular amino acid residue at position 211. The results indicate also that amino acid residues which appear to be functionally near-equivalent in one configuration may strongly influence the activity of a protein with a subsequent change at another site. Seven independent suppressors of trpA218 (Leu22-Ser211) were isolated. Their properties suggest that all seven may suppress the codon (AGU/C) for Ser211. Six of the seven are co-transducible with glyV , the structural gene for the GGU/C-specific tRNA Gly .

Bibliography

Murgola, E. J., & Yanofsky, C. (1974). Structural Interactions Between Amino Acid Residues at Positions 22 and 211 in the Tryptophan Synthetase Alpha Chain of Escherichia coli. Journal of Bacteriology, 117(2), 444–448.

Authors 2
  1. E. J. Murgola (first)
  2. C. Yanofsky (additional)
References 9 Referenced 51
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Dates
Type When
Created 5 years, 8 months ago (Jan. 3, 2020, 9:56 a.m.)
Deposited 4 years, 1 month ago (July 29, 2021, 1:11 p.m.)
Indexed 2 months ago (July 2, 2025, 2:48 p.m.)
Issued 51 years, 7 months ago (Feb. 1, 1974)
Published 51 years, 7 months ago (Feb. 1, 1974)
Published Print 51 years, 7 months ago (Feb. 1, 1974)
Funders 0

None

@article{Murgola_1974, title={Structural Interactions Between Amino Acid Residues at Positions 22 and 211 in the Tryptophan Synthetase Alpha Chain of Escherichia coli}, volume={117}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.117.2.444-448.1974}, DOI={10.1128/jb.117.2.444-448.1974}, number={2}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Murgola, E. J. and Yanofsky, C.}, year={1974}, month=feb, pages={444–448} }