Gap1 functions as a molecular chaperone to stabilize its interaction partner Gap3 during biogenesis of serine-rich repeat bacterial adhesin

Eitemau Tebyg

• A conserved domain of previously unknown function in Gap1 mediates protein-protein interaction and is required for biogenesis of a serine-rich streptococcal adhesin
  gan: Li, Yirong, et al.
  Cyhoeddwyd: (2008)
• Canonical SecA Associates with an Accessory Secretory Protein Complex Involved in Biogenesis of a Streptococcal Serine-Rich Repeat Glycoprotein
  gan: Zhou, Meixian, et al.
  Cyhoeddwyd: (2011)
• Engineering and Dissecting the Glycosylation Pathway of a Streptococcal Serine-rich Repeat Adhesin
  gan: Zhu, Fan, et al.
  Cyhoeddwyd: (2016)
• Interaction between Two Putative Glycosyltransferases Is Required for Glycosylation of a Serine-Rich Streptococcal Adhesin
  gan: Bu, Su, et al.
  Cyhoeddwyd: (2008)
• The pneumococcal serine-rich repeat protein is an intra-species bacterial adhesin that promotes bacterial aggregation in vivo and in biofilms.
  gan: Carlos J Sanchez, et al.
  Cyhoeddwyd: (2010-08-01)