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Architecture and roles of periplasmic adaptor proteins in tripartite e?ux assemblies.

ABSTRACT: Recent years have seen major advances in the structural understanding of the different components of tripartite e?ux assemblies, which encompass the multidrug e?ux (MDR) pumps and type I secretion systems. The majority of these investigations have focused on the role played by the inner membrane transporters and the outer membrane factor (OMF), leaving the third component of the system - the Periplasmic Adaptor Proteins (PAPs) - relatively understudied. Here we review the current state of knowledge of these versatile proteins which, far from being passive linkers between the OMF and the transporter, emerge as active architects of tripartite assemblies, and play diverse roles in the transport process. Recognition between the PAPs and OMFs is essential for pump assembly and function, and targeting this interaction may provide a novel avenue for combating multidrug resistance. With the recent advances elucidating the drug e?ux and energetics of the tripartite assemblies, the understanding of the interaction between the OMFs and PAPs is the last piece remaining in the complete structure of the tripartite pump assembly puzzle.

SUBMITTER: Symmons MF

PROVIDER: S-EPMC4446572 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Architecture and roles of periplasmic adaptor proteins in tripartite eﬄux assemblies.

Symmons Martyn F MF Marshall Robert L RL Bavro Vassiliy N VN

Frontiers in microbiology 20150528

Recent years have seen major advances in the structural understanding of the different components of tripartite eﬄux assemblies, which encompass the multidrug eﬄux (MDR) pumps and type I secretion systems. The majority of these investigations have focused on the role played by the inner membrane transporters and the outer membrane factor (OMF), leaving the third component of the system - the Periplasmic Adaptor Proteins (PAPs) - relatively understudied. Here we review the current state of knowle ...[more]

PMID: 26074901

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Project description:The ability to efficiently scavenge nutrients in the host is essential for the viability of any pathogen. All catabolic pathways must begin with the transport of substrate from the environment through the cytoplasmic membrane, a role executed by membrane transporters. Although several classes of cytoplasmic membrane transporters are described, high-affinity uptake of substrates occurs through Solute Binding-Protein (SBP) dependent systems. Three families of SBP dependant transporters are known; the primary ATP-binding cassette (ABC) transporters, and the secondary Tripartite ATP-independent periplasmic (TRAP) transporters and Tripartite Tricarboxylate Transporters (TTT). Far less well understood than the ABC family, the TRAP transporters are found to be abundant among bacteria from marine environments, and the TTT transporters are the most abundant family of proteins in many species of ?-proteobacteria. In this review, recent knowledge about these families is covered, with emphasis on their physiological and structural mechanisms, relating to several examples of relevant uptake systems in pathogenicity and colonization, using the SiaPQM sialic acid uptake system from Haemophilus influenzae and the TctCBA citrate uptake system of Salmonella typhimurium as the prototypes for the TRAP and TTT transporters, respectively. High-throughput analysis of SBPs has recently expanded considerably the range of putative substrates known for TRAP transporters, while the repertoire for the TTT family has yet to be fully explored but both types of systems most commonly transport carboxylates. Specialized spectroscopic techniques and site-directed mutagenesis have enriched our knowledge of the way TRAP binding proteins capture their substrate, while structural comparisons show conserved regions for substrate coordination in both families. Genomic and protein sequence analyses show TTT SBP genes are strikingly overrepresented in some bacteria, especially in the ?-proteobacteria and some ?-proteobacteria. The reasons for this are not clear but might be related to a role for these proteins in signaling rather than transport.

Dataset Information

Architecture and roles of periplasmic adaptor proteins in tripartite e?ux assemblies.

Publications

Architecture and roles of periplasmic adaptor proteins in tripartite eﬄux assemblies.

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