Glycolysis is one of the most important metabolic pathways in heterotrophic organisms. Several genes encoding glycolytic enzymes are essential in many bacteria even under conditions when neither glycolytic nor gluconeogenic activities are required. In this study, a screening for in vivo interaction partners of glycolytic enzymes of the soil bacterium Bacillus subtilis was used to provide a rationale for essentiality of glycolytic enzymes. Glycolytic enzymes proved to be in close contact with several other proteins, among them a high proportion of essential proteins. Among these essential interaction partners, other glycolytic enzymes were most prominent. Two-hybrid studies confirmed interactions of phosphofructokinase with phosphoglyceromutase and enolase. Such a complex of glycolytic enzymes might allow direct substrate channeling of glycolytic intermediates. Moreover we found associations of glycolytic enzymes with several proteins known or suspected to be involved in RNA processing and degradation. One of these proteins, Rny (YmdA), which has so far not been functionally characterized, is required for the processing of the mRNA of the glycolytic gapA operon. Two-hybrid analyses confirmed the interactions between the glycolytic enzymes phosphofructokinase and enolase and the enzymes involved in RNA processing, RNase J1, Rny, and polynucleotide phosphorylase. Moreover RNase J1 interacts with its homologue RNase J2. We suggest that this complex of mRNA processing and glycolytic enzymes is the B. subtilis equivalent of the RNA degradosome. Our findings suggest that the functional interaction of glycolytic enzymes with essential proteins may be the reason why they are indispensable. Glycolysis is a central metabolic pathway that appeared early in the evolution of life (1). Major functions of the glycolytic pathway are the generation of precursors for anabolic reactions and the conservation of energy that is needed to fuel all other cellular processes. The glycolytic pathway is conventionally divided into two parts: (i) the upper part, also referred to as the preparatory phase of glycolysis because the reactions of this part consume energy to convert the incoming sugars to triose phosphates, and (ii), the lower part or payoff phase that is characterized by the net gain of energy and the formation of reduction equivalents. Although glycolysis is highly conserved from archaea and bacteria to man not all organisms use this pathway for the oxidization of glucose. Escherichia coli is able to oxidize glucose via glycolysis, but the Entner-Doudoroff and the pentose phosphate pathways may replace the preparatory phase. In contrast to E. coli, the Entner-Doudoroff pathway is not present in Bacillus subtilis (2). Interestingly the enzymes of the upper glycolytic part seem to be completely absent in many archaea (3, 4). These few examples show that there is a high plasticity in how archaea and bacteria can feed glucose into the triose phosphate part of glycolysis. This plasticity is in good agreement with the observation that...
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