O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.

ABSTRACT: The serine-rich repeat (SRR) glycoproteins are a family of adhesins found in many Gram-positive bacteria. Expression of the SRR adhesins has been linked to virulence for a variety of infections, including streptococcal endocarditis. The SRR preproteins undergo intracellular glycosylation, followed by export via the accessory Sec (aSec) system. This specialized transporter is comprised of SecA2, SecY2 and three to five accessory Sec proteins (Asps) that are required for export. Although the post-translational modification and transport of the SRR adhesins have been viewed as distinct processes, we found that Asp2 of Streptococcus gordonii also has an important role in modifying the SRR adhesin GspB. Biochemical analysis and mass spectrometry indicate that Asp2 is an acetyltransferase that m

SUBMITTER: Seepersaud R 

PROVIDER: S-EPMC5578698 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature