Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 May 5;23(5):863–872. doi: 10.1016/j.str.2015.03.001

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2015 The Authors

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

PMC Copyright notice

Pseudoperiplasmic Localization of FlaF

(A) Dot far-western blot analysis of His₆-tagged sFlaF. Surface layer proteins (S-layer) isolated from S. acidocaldarius MW001 (WT), Δagl16, and Δagl3 strains were spotted on to an activated PVDF membrane and incubated with either sFlaF or with buffer. Binding of sFlaF with the S-layer was visualized using α-His antibodies. No specific signal was detected in the negative control. The panel on the right shows the N-glycan tree (Meyer and Albers, 2013) of the different strains. , N-acetyl glucosamine; , sulfoquinovose; ○, glucose; ●, mannose.

(B) Sedimentations assays were performed to analyze the interaction of sFlaF and the S-layer. FlaI was used as a negative control of the sedimentation assay. On the left, FlaI or FlaF were incubated alone. S and P indicate supernatant and pellet, respectively. In the two right lanes, FlaI and FlaF were incubated with the S-layer. Whereas FlaI shows no interaction with the S-layer, 50% of the FlaF was bound to the S-layer protein.

Inline graphic — Pseudoperiplasmic Localization of FlaF

(A) Dot far-western blot analysis of His₆-tagged sFlaF. Surface layer proteins (S-layer) isolated from S. acidocaldarius MW001 (WT), Δagl16, and Δagl3 strains were spotted on to an activated PVDF membrane and incubated with either sFlaF or with buffer. Binding of sFlaF with the S-layer was visualized using α-His antibodies. No specific signal was detected in the negative control. The panel on the right shows the N-glycan tree (Meyer and Albers, 2013) of the different strains. , N-acetyl glucosamine; , sulfoquinovose; ○, glucose; ●, mannose.

(B) Sedimentations assays were performed to analyze the interaction of sFlaF and the S-layer. FlaI was used as a negative control of the sedimentation assay. On the left, FlaI or FlaF were incubated alone. S and P indicate supernatant and pellet, respectively. In the two right lanes, FlaI and FlaF were incubated with the S-layer. Whereas FlaI shows no interaction with the S-layer, 50% of the FlaF was bound to the S-layer protein.