<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>Blagotinsek, Vitan</dc:creator>
  <dc:creator>Schwan, Meike</dc:creator>
  <dc:creator>Steinchen, Wieland</dc:creator>
  <dc:creator>Mrusek, Devid</dc:creator>
  <dc:creator>Hook, John C.</dc:creator>
  <dc:creator>Rossmann, Florian</dc:creator>
  <dc:creator>Freibert, Sven A.</dc:creator>
  <dc:creator>Kratzat, Hanna</dc:creator>
  <dc:creator>Murat, Guillaume</dc:creator>
  <dc:creator>Kressler, Dieter</dc:creator>
  <dc:creator>Beckmann, Roland</dc:creator>
  <dc:creator>Beeby, Morgan</dc:creator>
  <dc:creator>Thormann, Kai M.</dc:creator>
  <dc:creator>Bange, Gert</dc:creator>
  <dc:date>2020-08-25</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Bacterial flagella differ in their number and spatial arrangement. In many species, the  MinD-type ATPase FlhG (also YlxH/FleN) is central to the numerical control of  bacterial flagella, and its deletion in polarly flagellated bacteria typically leads to  hyperflagellation. The molecular mechanism underlying this numerical control,  however, remains enigmatic. Using the model species Shewanella putrefaciens, we  show that FlhG links assembly of the flagellar C ring with the action of the master  transcriptional regulator FlrA (named FleQ in other species). While FlrA and the  flagellar C-ring protein FliM have an overlapping binding site on FlhG, their binding  depends on the ATP-dependent dimerization state of FlhG. FliM interacts with FlhG  independent of nucleotide binding, while FlrA exclusively interacts with the ATP- dependent FlhG dimer and stimulates FlhG ATPase activity. Our in vivo analysis of  FlhG partner switching between FliM and FlrA reveals its mechanism in the numerical  restriction of flagella, in which the transcriptional activity of FlrA is down-regulated  through a negative feedback loop. Our study demonstrates another level of regulatory  complexity underlying the spationumerical regulation of flagellar biogenesis and  implies that flagellar assembly transcriptionally regulates the production of more initial  building blocks.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/309059</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/309059/files/kre_adp.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/309059/files/kre_adp_sm.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.2006470117</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Proceedings of the National Academy of Sciences. - 2020, vol. 117, no. 34, p. 20826–20835</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">An ATP-dependent partner switch links flagellar C-ring assembly with gene expression</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
