Protease-associated import systems are widespread in Gram-negative bacteria


Autoři: Rhys Grinter aff001;  Pok Man Leung aff001;  Lakshmi C. Wijeyewickrema aff004;  Dene Littler aff002;  Simone Beckham aff002;  Robert N. Pike aff004;  Daniel Walker aff006;  Chris Greening aff001;  Trevor Lithgow aff002
Působiště autorů: School of Biological Sciences, Monash University, Clayton, Victoria, Australia aff001;  Infection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton, Australia aff002;  Institute of Microbiology and Infection, School of Immunity and Infection, University of Birmingham, Birmingham, England, United Kingdom aff003;  Department of Biochemistry and Genetics, La Trobe Institute of Molecular Sciences, La Trobe University, Melbourne, Victoria, Australia aff004;  La Trobe Rural Health School, College of Science, Health and Engineering, La Trobe University, Bendigo, Australia aff005;  Institute of Infection, Immunity, and Inflammation, College of Medical, Veterinary, and Life Sciences, University of Glasgow, Glasgow, United Kingdom aff006
Vyšlo v časopise: Protease-associated import systems are widespread in Gram-negative bacteria. PLoS Genet 15(10): e32767. doi:10.1371/journal.pgen.1008435
Kategorie: Research Article
doi: 10.1371/journal.pgen.1008435

Souhrn

Bacteria have evolved sophisticated uptake machineries in order to obtain the nutrients required for growth. Gram-negative plant pathogens of the genus Pectobacterium obtain iron from the protein ferredoxin, which is produced by their plant hosts. This iron-piracy is mediated by the ferredoxin uptake system (Fus), a gene cluster encoding proteins that transport ferredoxin into the bacterial cell and process it proteolytically. In this work we show that gene clusters related to the Fus are widespread in bacterial species. Through structural and biochemical characterisation of the distantly related Fus homologues YddB and PqqL from Escherichia coli, we show that these proteins are analogous to components of the Fus from Pectobacterium. The membrane protein YddB shares common structural features with the outer membrane ferredoxin transporter FusA, including a large extracellular substrate binding site. PqqL is an active protease with an analogous periplasmic localisation and iron-dependent expression to the ferredoxin processing protease FusC. Structural analysis demonstrates that PqqL and FusC share specific features that distinguish them from other members of the M16 protease family. Taken together, these data provide evidence that protease associated import systems analogous to the Fus are widespread in Gram-negative bacteria.

Klíčová slova:

Crystal structure – Crystals – Glycerol – Operons – Outer membrane proteins – Proteases – Sequence databases – Sequence similarity searching


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Genetika Reprodukční medicína

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PLOS Genetics


2019 Číslo 10

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