<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>Rohrer S</dc:creator>
  <dc:creator>Berger-Bächi B</dc:creator>
  <dc:date>2003</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Protein-protein interactions play an important role in all cellular processes. The development of two-hybrid systems in yeast and bacteria allows for in vivo assessment of such interactions. Using a recently developed bacterial two-hybrid system, the interactions of the Staphylococcus aureus proteins FemA, FemB and FmhB, members of the FemABX protein family, which is involved in peptidoglycan biosynthesis and beta-lactam resistance of numerous Gram-positive bacteria, were analysed. While FmhB is involved in the addition of glycine 1 of the pentaglycine interpeptide of S. aureus peptidoglycan, FemA and FemB are specific for glycines 2/3 and 4/5, respectively. FemA-FemA, FemA-FemB and FemB-FemB interactions were found, while FmhB exists solely as a monomer. Interactions detected by the bacterial two-hybrid system were confirmed using the glutathione S-transferase-pulldown assay and gel filtration.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/235965</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.26315-0</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/14523106</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Microbiology (Reading, England). - 2003</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Bacterial Proteins</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Chromatography, Gel</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Dimerization</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Molecular Weight</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Staphylococcus</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Two-Hybrid System Techniques</dc:subject>
  <dc:title xmlns:ns7="xml" ns7:lang="en">Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
