A conserved domain of previously unknown function in Gap1 mediates protein-protein interaction and is required for biogenesis of a serine-rich streptococcal adhesin

Lignende værker

• Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin
  af: Bu, Su, et al.
  Udgivet: (2008)
• Gap1 functions as a molecular chaperone to stabilize its interaction partner Gap3 during biogenesis of serine-rich repeat bacterial adhesin
  af: Zhou, Meixian, et al.
  Udgivet: (2012)
• A Novel Glucosyltransferase Is Required for Glycosylation of a Serine-rich Adhesin and Biofilm Formation by Streptococcus parasanguinis
  af: Zhou, Meixian, et al.
  Udgivet: (2010)
• A Conserved C-Terminal 13-Amino-Acid Motif of Gap1 Is Required for Gap1 Function and Necessary for the Biogenesis of a Serine-Rich Glycoprotein of Streptococcus parasanguinis
  af: Zhou, Meixian, et al.
  Udgivet: (2008)
• Canonical SecA Associates with an Accessory Secretory Protein Complex Involved in Biogenesis of a Streptococcal Serine-Rich Repeat Glycoprotein
  af: Zhou, Meixian, et al.
  Udgivet: (2011)