Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec System.

Abstract:

:GspB is a serine-rich glycoprotein adhesin of Streptococcus gordonii that is exported to the bacterial surface by the accessory Sec system. This dedicated export pathway is comprised of seven components (SecA2, SecY2, and five accessory Sec proteins [Asp1 to Asp5]). The latter proteins have no known homologs beyond the Asps of other species. Asp1 to Asp3 are absolutely required for export of the substrate GspB, but their roles in this process are unknown. Using copurification analysis and far-Western blotting, we found that Asp2 and Asp3 could individually bind the serine-rich repeat (SRR) domains of GspB. Deletion of both SRR regions of GspB led to a decrease in its export, suggesting that binding of the Asps to the SRR regions is important for GspB transport by the accessory Sec system. The Asps also bound a heterologous substrate for the accessory Sec system containing a slow-folding MalE variant, but they did not bind wild-type MalE. The combined results indicate that the Asps may recognize the export substrate through preferential interactions with its unstructured or unfolded regions. Glycosylation of the SRR domains on GspB prevented Asp binding, suggesting that binding of the Asps to the preprotein occurs prior to its full glycosylation. Together, these findings suggest that Asp2 and Asp3 are likely to function in part as chaperones in the early phase of GspB transport.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Yen YT,Seepersaud R,Bensing BA,Sullam PM

doi

10.1128/JB.00057-11

subject

Has Abstract

pub_date

2011-07-01 00:00:00

pages

3165-74

issue

13

eissn

0021-9193

issn

1098-5530

pii

JB.00057-11

journal_volume

193

pub_type

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