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Published Erratum
. 2015 Sep 22;112(38):E5371-5.
doi: 10.1073/pnas.1516042112. Epub 2015 Aug 31.

Correction for Hobley et al., BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm

No authors listed
Published Erratum

Correction for Hobley et al., BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm

No authors listed. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 6.
Fig. 6.
In vivo biofilm analysis of the hydrophobic cap of BslA. (A) Complex colony morphologies of strains containing leucine/isoleucine-to-lysine mutations in the β-sheets CAP2 and CAP3 alongside wild-type (NCIB3610), bslA− (NRS2097), and bslA+ (NRS2299) controls. (B) Pellicle morphology of the CAP2 and CAP3 mutants shown in A. (C) Sessile water-drop analysis of colony hydrophobicity of CAP2 and CAP3 mutants. Colonies were grown as for morphology analysis and 5-µL water drops placed on top. (D) Complex colony morphologies of strains containing mutations in the central CAP1 β-sheet. (E) Pellicle morphology of the CAP1 mutants shown in D. (F) Water-droplet analysis of colony hydrophobicity of CAP1 mutants. Table S3 gives strain details.
Fig. S5.
Fig. S5.
Protein production and stability of in vivo BslA hydrophobic cap mutants. Western blot analysis using a BslA-specific primary antibody of protein extracted from whole complex colonies of (A) CAP2 and CAP3 mutants (as shown in Fig. 6A) and (B) CAP1 mutants (Fig. 6D). Colonies were grown for 48 h at 30 °C before extraction. (C) Pellicles of CAP1 mutant strains, grown for 18 h at 37 °C, were separated into pellicle (P, containing both cells and the biofilm matrix) and media (M) fractions. Western blots were probed with a BslA-specific primary antibody. Pellicles with wild-type morphology show that most BslA protein is found within the P fraction, whereas those with altered pellicle morphology have BslA protein in both the P and M fractions. When BslA is present in the media a second, lower-molecular-weight degradation product appears.
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