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Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae.
J Bacteriol. 1993 Feb; 175(4):1061-8.JB

Abstract

The initial step of tryptophan biosynthesis is catalyzed by the enzyme anthranilate synthase, which in most microorganisms is subject to feedback inhibition by the end product of the pathway. We have characterized the TRP2 gene from a mutant Saccharomyces cerevisiae strain coding for an anthranilate synthase that is unresponsive to tryptophan. Sequence analysis of this TRP2(Fbr) (feedback-resistant) allele revealed numerous differences from a previously published TRP2 sequence. However, TRP2(Fbr) was found to differ in only one single-point mutation from its own parent wild type, a C-to-T transition resulting in a serine 76-to-leucine 76 amino acid substitution. Therefore, serine 76 is a crucial amino acid for proper regulation of the yeast enzyme. We constructed additional feedback-resistant enzyme forms of the yeast anthranilate synthase by site-directed mutagenesis of the conserved LLES sequence in the TRP2 gene. From analysis of these variants, we propose an extended sequence, LLESX10S, as the regulatory element in tryptophan-responsive anthranilate synthases from prokaryotic and eukaryotic organisms.

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Authors+Show Affiliations

Graf R
Institute of Microbiology, Swiss Federal Institute of Technology, Zurich.
Mehmann B
No affiliation info available
Braus GH
No affiliation info available

MeSH

Amino Acid SequenceAnthranilate SynthaseBase SequenceFeedbackGene Expression Regulation, FungalGenes, FungalMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesSaccharomyces cerevisiaeSequence AlignmentStructure-Activity Relationship

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8432699

Citation

Graf, R, et al. "Analysis of Feedback-resistant Anthranilate Synthases From Saccharomyces Cerevisiae." Journal of Bacteriology, vol. 175, no. 4, 1993, pp. 1061-8.
Graf R, Mehmann B, Braus GH. Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae. J Bacteriol. 1993;175(4):1061-8.
Graf, R., Mehmann, B., & Braus, G. H. (1993). Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae. Journal of Bacteriology, 175(4), 1061-8.
Graf R, Mehmann B, Braus GH. Analysis of Feedback-resistant Anthranilate Synthases From Saccharomyces Cerevisiae. J Bacteriol. 1993;175(4):1061-8. PubMed PMID: 8432699.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae. AU - Graf,R, AU - Mehmann,B, AU - Braus,G H, PY - 1993/2/1/pubmed PY - 1993/2/1/medline PY - 1993/2/1/entrez SP - 1061 EP - 8 JF - Journal of bacteriology JO - J Bacteriol VL - 175 IS - 4 N2 - The initial step of tryptophan biosynthesis is catalyzed by the enzyme anthranilate synthase, which in most microorganisms is subject to feedback inhibition by the end product of the pathway. We have characterized the TRP2 gene from a mutant Saccharomyces cerevisiae strain coding for an anthranilate synthase that is unresponsive to tryptophan. Sequence analysis of this TRP2(Fbr) (feedback-resistant) allele revealed numerous differences from a previously published TRP2 sequence. However, TRP2(Fbr) was found to differ in only one single-point mutation from its own parent wild type, a C-to-T transition resulting in a serine 76-to-leucine 76 amino acid substitution. Therefore, serine 76 is a crucial amino acid for proper regulation of the yeast enzyme. We constructed additional feedback-resistant enzyme forms of the yeast anthranilate synthase by site-directed mutagenesis of the conserved LLES sequence in the TRP2 gene. From analysis of these variants, we propose an extended sequence, LLESX10S, as the regulatory element in tryptophan-responsive anthranilate synthases from prokaryotic and eukaryotic organisms. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/8432699/Analysis_of_feedback_resistant_anthranilate_synthases_from_Saccharomyces_cerevisiae_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=8432699 DB - PRIME DP - Unbound Medicine ER -