<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Wang J</dc:creator>
  <dc:creator>Brodmann M</dc:creator>
  <dc:creator>Basler M</dc:creator>
  <dc:date>2019</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Bacteria need to deliver large molecules out of the cytosol to the extracellular space or even across membranes of neighboring cells to influence their environment, prevent predation, defeat competitors, or communicate. A variety of protein-secretion systems have evolved to make this process highly regulated and efficient. The type VI secretion system (T6SS) is one of the largest dynamic assemblies in gram-negative bacteria and allows for delivery of toxins into both bacterial and eukaryotic cells. The recent progress in structural biology and live-cell imaging shows the T6SS as a long contractile sheath assembled around a rigid tube with associated toxins anchored to a cell envelope by a baseplate and membrane complex. Rapid sheath contraction releases a large amount of energy used to push the tube and toxins through the membranes of neighboring target cells. Because reach of the T6SS is limited, some bacteria dynamically regulate its subcellular localization to precisely aim at their targets and thus increase efficiency of toxin translocation.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/51314</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1146/annurev-micro-020518-115420</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/31226022</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Annual review of microbiology. - 2019</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">bacterial secretion systems</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">contractile nanomachines</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">sensing and signaling cascades</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">subcellular localization</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Bacterial Proteins</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Bacterial Secretion Systems</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Cell Membrane</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Escherichia coli</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Escherichia coli Proteins</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Gram-Negative Bacteria</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Lipoproteins</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Signal Transduction</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Type VI Secretion Systems</dc:subject>
  <dc:title xmlns:ns14="xml" ns14:lang="en">Assembly and Subcellular Localization of Bacterial Type VI Secretion Systems.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
