The RNA degradosome is a conglomerate of proteins responsible for the degradation of most mRNA transcripts in the prokaryotic cell. The present work was motivated by the need to better understand whether the RNA degradosome in Vibrio angustum S14 is similar or different to the RNA degradosome in Escherichia coli. V. angustum S14 is a model organism for the study of starvation and stress resistance, and shows global stabilisation of transcripts during these unique processes. There are two major aims to this work – the first, is to characterise the RNA degradosome in V. angustum S14, the second is to determine whether the RNA degradosome undergoes remodelling in response to starvation conditions. Two different paths were taken to study the RNA degradosome of V. angustum S14. Firstly, sequence comparisons and computer programs were used to predict the potential interaction sites of RNase E with the degradosome proteins. Secondly, we used a combination of genetic and biochemical methods to study the interactions of RhlB, enolase and PNPase with V. angustum S14 RNase E. Based on sequence homology, we predicted that V. angustum S14 RNase E possesses catalytic function and this was demonstrated through complementation of E. coli temperature sensitive mutants. We identified microdomains in the V. angustum S14 RNase E CTH and demonstrated their interactions with RhlB, enolase and PNPase using two-hybrid analysis. Further, through affinity chromatography and immunoprecipitation, the biochemical interactions between RNase E and the degradosome proteins were confirmed. In the first study of its kind, we then used Blue-Native PAGE to investigate the RNA degradosome. During starvation, we observed the levels of degradosome proteins to be stable. However, we did observe the induction of a truncated RhlB on the onset of starvation. These observations challenge earlier views on the role of the degradosome in starved V. angustum S14 cells. Finally, the implications of our findings are discussed.