Sugar metabolism and regulation in the hyperthermophilic archaeon Thermococcus litoralis
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Zusammenfassung
A novel trehalose glycosyl transferring synthase (TreT) from the hyperthermophilic archaeon T. litoralis was identified. This enzyme produces trehalose by the transfer of glucose from ADP-glucose (or, less effectively, UDP-glucose and GDP-glucose) onto the 1-position of glucose to form trehalose and ADP. Such an enzymatic activity in the synthesis of trehalose has not yet been described for any other organisms. It catalyzes a reversible reaction for trehalose synthesis and degradation by converting glucose and ADP-glucose to trehalose and ADP. The enzyme properties were characterized biochemically. The physiological function of TreT in vivo is still not completely understood.
An ATP-dependent and fructose-6-phosphate-forming fructokinase (Frk) was also identified and characterized in T. litoralis, which gene locates divergently to the trehalose/maltose transporter. The biochemical properties of this enzyme were characterized in this study.
TrmB is a novel archaeal sugar-specific transcriptional repressor regulating the expression of trehalose/maltose ABC transporter dependent on the presence of maltose or trehalose in medium. TrmB binds maltose much stronger than trehalose. TrmB binds to the DNA fragments of the TATA box promoter region and upstream motif of malEFG-operon. TrmB does not bind to MalK.
Two enzymes (TreT and FrK) have been identified in this research work and their expressional regulation by TrmB also has been investigated. The further interesting work can focus on the sucrose or trehalose metabolism pathway and the net work of sugar metabolism regulation in T. litoralis.
Zusammenfassung in einer weiteren Sprache
Die Arbeit enthält die molekulare und biochemische Beschreibung von drei Genprodukten aus dem hyperthermophilen Archaeon Thermococcus litoralis. Die entprechenden Gene gehören zu einem Cluster, dessen Funktion die Aufnahme und der Stoffwechsel von Maltose und Trehalose ist.
Das erste Protein (TreT) ist eine neuartige Glucosyl-transferierende Trehalosesynthase, die den Glucosylrest von ADP-Glucose auf freie Glucose überträgt und dabei Trehalose synthetisiert. Diese Enzymaktivität wurde bisher noch in keinem Organismus beschrieben. Die Reaktion ist reversibel; das Enzym katalysiert auch die Spaltung von Trehalose mit Hilfe von ADP und unter Bildung von Glucose und ADP-Glucose. Die physiologische Rolle des Enzyms ist noch unklar, aber mehrere Gründe sprechen dafür, dass TreT am Abbau von Trehalose beteiligt ist.
Das zweite Enzym (Frk) ist eine Fructokinase, die Fructose unter ATP-Spaltung zu Fructose-6-Phosphat phosphoryliert. Es ist das erste Enzym dieser Art, das in Archaea beschrieben wurde.
Das dritte Protein ist TrmB. Es hat keine enzymatische Funktion, ist aber an der Regulation der Genexpression beteiligt: es reguliert sowohl die Expression des malEFG-Operons wie auch die seines eigenen Gens. Es wurden Bindungsstudien von TrmB an die Promoterregion des Operons durchgeführt, ebenso Bindungsstudien von Trehalose und Maltose an TrmB. Beide Zucker wirken in vivo als Induktoren des Systems, was TrmB als einen transkriptionellen Repressor des Systems charakterisiert.
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QU, Qiuhao, 2004. Sugar metabolism and regulation in the hyperthermophilic archaeon Thermococcus litoralis [Dissertation]. Konstanz: University of KonstanzBibTex
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<dcterms:abstract xml:lang="eng">A novel trehalose glycosyl transferring synthase (TreT) from the hyperthermophilic archaeon T. litoralis was identified. This enzyme produces trehalose by the transfer of glucose from ADP-glucose (or, less effectively, UDP-glucose and GDP-glucose) onto the 1-position of glucose to form trehalose and ADP. Such an enzymatic activity in the synthesis of trehalose has not yet been described for any other organisms. It catalyzes a reversible reaction for trehalose synthesis and degradation by converting glucose and ADP-glucose to trehalose and ADP. The enzyme properties were characterized biochemically. The physiological function of TreT in vivo is still not completely understood.<br />An ATP-dependent and fructose-6-phosphate-forming fructokinase (Frk) was also identified and characterized in T. litoralis, which gene locates divergently to the trehalose/maltose transporter. The biochemical properties of this enzyme were characterized in this study.<br />TrmB is a novel archaeal sugar-specific transcriptional repressor regulating the expression of trehalose/maltose ABC transporter dependent on the presence of maltose or trehalose in medium. TrmB binds maltose much stronger than trehalose. TrmB binds to the DNA fragments of the TATA box promoter region and upstream motif of malEFG-operon. TrmB does not bind to MalK.<br />Two enzymes (TreT and FrK) have been identified in this research work and their expressional regulation by TrmB also has been investigated. The further interesting work can focus on the sucrose or trehalose metabolism pathway and the net work of sugar metabolism regulation in T. litoralis.</dcterms:abstract>
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