Dataset Information

Enzyme IIA^Ntr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism.

ABSTRACT: Many Proteobacteria possess a nitrogen-metabolic phosphotransferase system (PTS^Ntr) consisting of EI^Ntr, NPr, and EIIA^Ntr (encoded by ptsP, ptsO, and ptsN, respectively). The PTS^Ntr plays diverse regulatory roles, but the substrate phosphorylated by EIIA^Ntr and its primary functions have not yet been identified. To comprehensively understand the roles of PTS^Ntr in Salmonella Typhimurium, we compared the whole transcriptomes of wild-type and a ΔptsN mutant. Genome-wide RNA sequencing revealed that 3.5% of the annotated genes were up- or down-regulated by three-fold or more in the absence of EIIA^Ntr. The ΔptsN mutant significantly down-regulated the expression of genes involved in vitamin B₁₂ synthesis, 1,2-propanediol utilization, and propionate catabolism. Moreover, the invasiveness of the ΔptsN mutant increased about 5-fold when 1,2-propanediol or propionate was added, which was attributable to the increased stability of HilD, the transcriptional regulator of Salmonella pathogenicity island-1. Interestingly, an abundance of 1,2-propanediol or propionate promoted the production of EIIA^Ntr, suggesting the possibility of a positive feedback loop between EIIA^Ntr and two catabolic pathways. These results demonstrate that EIIA^Ntr is a key factor for the utilization of 1,2-propanediol and propionate as carbon and energy sources, and thereby modulates the invasiveness of Salmonella via 1,2-propanediol or propionate catabolism.

SUBMITTER: Yoo W

PROVIDER: S-EPMC5363084 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Publications

Enzyme IIANtr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism.

Yoo Woongjae W Kim Dajeong D Yoon Hyunjin H Ryu Sangryeol S

Scientific reports 20170323

Many Proteobacteria possess a nitrogen-metabolic phosphotransferase system (PTSNtr) consisting of EINtr, NPr, and EIIANtr (encoded by ptsP, ptsO, and ptsN, respectively). The PTSNtr plays diverse regulatory roles, but the substrate phosphorylated by EIIANtr and its primary functions have not yet been identified. To comprehensively understand the roles of PTSNtr in Salmonella Typhimurium, we compared the whole transcriptomes of wil ...[more]

PMID: 28333132

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Project description:Bacterial microcompartments (MCPs) are protein-based organelles that house the enzymatic machinery for metabolism of niche carbon sources, allowing enteric pathogens to outcompete native microbiota during host colonization. While much progress has been made toward understanding MCP biogenesis, questions still remain regarding the mechanism by which core MCP enzymes are enveloped within the MCP protein shell. Here, we explore the hypothesis that the shell protein PduB is responsible for linking the shell of the 1,2-propanediol utilization (Pdu) MCP from Salmonella enterica serovar Typhimurium LT2 to its enzymatic core. Using fluorescent reporters, we demonstrate that all members of the Pdu enzymatic core are encapsulated in Pdu MCPs. We also demonstrate that PduB is critical for linking the entire Pdu enzyme core to the MCP shell. Using MCP purifications, transmission electron microscopy, and fluorescence microscopy, we find that shell assembly can be decoupled from the enzymatic core, as apparently empty MCPs are formed in Salmonella strains lacking PduB. Mutagenesis studies reveal that PduB is incorporated into the Pdu MCP shell via a conserved, lysine-mediated hydrogen bonding mechanism. Finally, growth assays and system-level pathway modeling reveal that unencapsulated pathway performance is strongly impacted by enzyme concentration, highlighting the importance of minimizing polar effects when conducting these functional assays. Together, these results provide insight into the mechanism of enzyme encapsulation within Pdu MCPs and demonstrate that the process of enzyme encapsulation and shell assembly are separate processes in this system, a finding that will aid future efforts to understand MCP biogenesis. IMPORTANCE MCPs are unique, genetically encoded organelles used by many bacteria to survive in resource-limited environments. There is significant interest in understanding the biogenesis and function of these organelles, both as potential antibiotic targets in enteric pathogens and also as useful tools for overcoming metabolic engineering bottlenecks. However, the mechanism by which these organelles are formed natively is still not completely understood. Here, we provide evidence of a potential mechanism in S. enterica by which a single protein, PduB, links the MCP shell and metabolic core. This finding is critical for those seeking to disrupt MCPs during pathogenic infections or for those seeking to harness MCPs as nanobioreactors in industrial settings.

Dataset Information

Enzyme IIA^Ntr Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism.

Publications

Enzyme IIA<sup>Ntr</sup> Regulates Salmonella Invasion Via 1,2-Propanediol And Propionate Catabolism.

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