Research Collection. Doctoral Thesis. ETH Library. Author(s): Graf, Roney. Publication Date: 1994
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1 Research Collection Doctoral Thesis Anthranilate synthase and chorismate mutase allosteric regulation of two branchpoint enzymes from the aromatic amino acid biosynthetic pathway of the yeast Saccharomyces cerevisiae Author(s): Graf, Roney Publication Date: 1994 Permanent Link: Rights / License: In Copyright - Non-Commercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library
2 Diss ETH No ANTHRANILATE SYNTHASE AND CHORISMATE MUTASE: ALLOSTERIC REGULATION OF TWO BRANCHPOINT ENZYMES FROM THE AROMATIC AMINO ACID BlOSYNTHETIC PATHWAY OF THE YEAST SACCHAROMYCES CEREVISIAE A dissertation submitted to the SWISS FEDERAL INSTITUTE OF TECHNOLOGY (ETH) ZURICH, Switzerland for the degree of a Doctor of Natural Sciences presented by roney Graf Dipl. Narw. ETH born March 4,1966 citizen of Unterengstringen (ZH) accepted on the recommendation of Prof. Dr. Ralf Hurler, examiner Prof. Dr. Gerhard H. Braus, co-examiner Prof. Dr. Hauke Hennecke, co-examiner Zurich 1994 i2,w.uii m
3 1 SUMMARY The regulation of two enzymes competing for a common substrate in the aromatic amino acid biosynthetic pathway in the yeast Saccharomyces cerevisiae was investigated. Anthranilate synthase (E.C ) and chorismate mutase (E.C ), both using chorismic acid for the first steps of tryptophan or tyrosine/phenylalanine biosynthesis, respectively, form the central branchpoint in this metabolic pathway and are therefore important targets for regulation. Anthranilate synthase, catalysing the first step of the tryptophan-specific branch, is formed by the gene products of TRP2 and TRP3. Whereas the wildtype enzyme is feedback inhibited by the end product of the pathway, tryptophan, a mutant allele of TRP2 encodes a feedback-resistant enzyme. The analysis of this TRP2fl>r allele revealed a single point mutation leading to a serine-to-leucine exchange at position 76 of the protein. Serine 76 was found to be a highly conserved residue in all anthranilate synthases analysed so far. Its proximity to another conserved element, comprising another serine known to be involved in tryptophan regulation, suggested the presence of an extended tryptophanregulatory element with the sequence LLESSS-Xio-S7*. The site-directed exchange of the upstream serine 65 to arginine led to an equivalent reduction of feedback sensitivity of the enzyme as the TRP2ft* mutation in serine 76, and this effect was not found to be enhanced in a construct carrying both mutations. Therefore, it was concluded that both serines are part of the same functional element. Chorismate mutase, the product of the AR07 gene, is responsible for the first reaction of the tyrosine/phenylalanine-specific branch. The homodimeric enzyme is subject to feedback inhibition by tyrosine and to a 'cross-branch'- activation by tryptophan. Its kinetic behaviour conforms the classical Monod- Wyman-Changeux model for allosteric enzymes. A point mutation causing a threonine-to-isoleucine exchange in residue 226 and leading to a constitutively activated enzyme (AR07c) was found to be frozen in the active allosteric R-state. A set of new mutations in codon 226 of the AR07 gene was created, and the kinetic behaviour of the nine resulting enzymes was analysed. The determination of their steady-state kinetic parameters led to the following observations: a) None of the exchanges at residue 226 affected the catalytic constant of the enzyme, b) All mutations led to a specific activation of the enzyme by decreasing Km, along with a decreasing response to the inhibitor tyrosine and a decreasing cooperativity of substrate binding, c) The strength of the
4 although 2 deregulation did not correlate with any characteristic of the artificially introduced amino acid at position 226. The data are consistent with a gradual shifting allosteric of the T-R-equilibrium of the enzyme towards the R-state by the various mutations. This model was tested and confirmed by in vitro ligand binding studies of tyrosine and tryptophan to the mutant enzymes. Closely downstream of the AR07 gene encoding chorismate mutase, the 3'- end of an open reading frame with similarities to a superfamily of membrane proteins was detected. The presence of a transcript was shown, the entire gene was cloned and sequenced, and a disruption mutant was constructed. Sequence comparisons indicated that the new gene encodes a putative mitochondrial carrier protein and was therefore named YMCl. A phenotype for the disruption mutant could not be detected. In particular, it phenotype - associated with the AR07 locus was shown that the osmosensitive unexplainable - so far is indeed triggered by inactivation of the AR07 gene and not by its neighbour YMCl.
5 3 ZUSAMMENFASSUNG Gegenstand dieser Untersuchungen war die Regulation der beiden Enzyme, welche in der aromatischen Aminosaurebiosynthese in der Hefe Saccharomyces cerevisiae um das gemeinsame Substrat Chorisminsaure konkurrieren. Anthranilatsynthase (E.C ) und Chorismarmutase (E.C ), die jeweils den ersten spezifischen Schritt der Synthese von Tryptophan beziehungsweise Tyrosin und Phenylalanin katalysieren, zentralen Verzweigungspunkt in diesem Biosyntheseweg wichtige Punkte in dessen Regulation. befinden sich am und sind daher Anthranilatsynthase katalysiert den ersten Schritt des Tryptophanspezifischen Astes und wird von den Produkten der Gene TRP2 und TRP3 gebildet. WShrend das Enzym in der Wildtypform durch Tryptophan gehemmt wird, zeigt das Produkt des Mutantenallels TRP2fl» (furfeedback-resistant) keine Endprodukthemmung. identifiziert Im TRP2fl>r-Gen konnte eine einzelne Punktmutation werden, die einen Austausch eines Serins an Position 76 gegen Leucin bewirkt. Dieses Serin 76 ist in alien bekannten Anthranilatsynthasen weitgehend konserviert, und da es in der Nahe eines anderen, ebenfalls konservierten und in der Regulation durch Tryptophan involvierten Bereiches liegt, wurde ein erweitertes regulatorisches Element mit der Sequenz LLES65-Xio- S76 postuliert. Ein gezielter Austausch von Serin 76 bewirkte eine gleichwertige Verminderung der Regulierbarkeit des Enzyms durch Tryptophan wie die TRPZ/^-Mutation in Serin 65, und dieser Effekt konnte durch den gleichzeitigen Austausch beider Serinpositionen nicht mehr verstarkt werden. Daraus wurde geschlossen, dass sowohl Serin 65 als auch Serin 76 Teile eines einzigen Tryptophan-regulatorischen Elementes sind. Chorismarmutase, bestehend aus zwei Einheiten des AR07-Genproduktes, ist fur die Katalyse der ersten Reaktion des Tyrosin-/Phenylalanin-spezifischen Astes verantwortlich. Das Enzym wird einerseits durch Tyrosin gehemmt, andererseits durch Tryptophan aktiviert. Ihr kinetisches Verhalten lasst sich mit dem Monod-Wyman-Changeux-Modell fiir allosteriche Enzyme beschreiben. Eine Punktmutation (AR07c), die einen Austausch eines Threonins gegen Isoleucin an Position 226 bewirkt und sich in einem konstitutiv aktivierten Enzym aussert, friert das Enzym im aktiven allosterischen R-Zustand ein. Daher wurde eine Serie weiterer Aminosaure-Austausche an der Stelle 226 durchgefuhrt, und die kinetischen Daten der resultierenden neun Enzymspezies
6 4 bestimmt. Dabei wurden folgende Beobachtungen gemacht: a) Keine der Mutationen hatte einen Einfluss auf die katalytische Konstante der Chorismatmutase. b) Alle Mutationen bewirkten eine Aktivierung des Enzyms durch Senkung des Km, sowie eine Abnahme der Hemmbarkeit durch Tyrosin und der Kooperativitat bezuglich der Substratbindung. c) Die Starke des beobachteten Effektes korrelierte mit keiner spezifischen Eigenschaft der entsprechenden kunstlich eingefiihrten Aminosaure an Position 226. Diese Ergebnisse lassen sich so erklaren, dass die verschiedenen Mutationen jeweils eine Verschiebung des allosterischen T-R-Gleichgewichts in unterschiedlicher Starke zur R-Seite hin bewirken. Dieses Modell wurde durch in vitro Bindungsstudien von Tyrosin und Tryptophan an die mutierten Enzyme uberpruft und bestatigt. Nahe des 3'-Endes des AR07-Gens, welches fur Chorismatmutase kodiert, wurde ein offener Leseraster entdeckt, der Homologien zu einer Superfamilie von Membranproteinen aufweist. Ein entsprechendes Transkript konnte daraufhin nachgewiesen werden, das vollstandige Gen wurde kloniert und sequenziert und eine Mutante durch Gen-Disruption konstruiert. Aus Sequenzvergleichen wurde geschlossen, dass dieses Gen vermutlich fiir ein mitochondriales Transportprotein kodiert. Es erhielt daher die Bezeichnung YMCl, fur yeast mitochondrial carrier. Ein besonderer Phanotyp der Mutante konnte nicht beobachtet werden. Insbesondere wurde nachgewiesen, dass die noch unerklarte Osmosensitivitat, welche mit Mutationen im Bereich des AR07- Locus einhergeht, tatsachlich mit dem AR07-Gen selbst und nicht mit dem benachbarten YMCl-Gen assoziiert ist.
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Research Collection Doctoral Thesis Globale Symmetrie von stochastischen Teilchenbewegungen mit lokal symmetrischer Interaktion Author(s): Barner, Andreas Publication Date: 1983 Permanent Link: https://doi.org/10.3929/ethz-a-000294972
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Research Collection Doctoral Thesis The microsomal monooxygenase system interactions of the components Author(s): Kunz, Barbara Claudia Publication Date: 1986 Permanent Link: https://doi.org/10.3929/ethza000404439
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MehrVerallgemeinerungen des Herbrand'schen Satzes und Anwendungen im Gebiet der Entscheidbarkeit von Formelklassen
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MehrPsoriatic fibroblasts in cell culture contribution to the mode of action of fumarates in psoriasis treatment
Research Collection Doctoral Thesis Psoriatic fibroblasts in cell culture contribution to the mode of action of fumarates in psoriasis treatment Author(s): Sarheim, Berit Sveine Publication Date: 1990
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