| Autor: |
Green, Charlotte, Nitin S. Kamble, Court, Elizabeth K., Bryant, Owain, Hicks, Matthew G., Lennon, Christopher, Fraser, Gillian, Wright, Phillip, Stafford, Graham |
| Rok vydání: |
2019 |
| DOI: |
10.6084/m9.figshare.7607900.v1 |
| Popis: |
Additional file 1: Table S1. Escherichia coli strains used or generated in this study. Table S2. Plasmids used or generated in this study. Table S3. Polymerase chain reaction primers used in the study. Fig. S1. Annotation of the genetic region upstream of the flhD operon in E. coli MC1000. Fig. S2. Comparison of growth of the HAP-less and cap-less strains. Growth curve data for the aforementioned strains. Fig. S3. Functional flagellar despite the absence of the FliC D3 domain. SDS-PAGE of secreted protein and motility assay. Fig. S4. The effect of the deletion of clpX from E. coli MC1000. Comparison of the strains by: abundance of secreted flagellin, motility assay and phenotype. Fig. S5. Plasmid maps of (a) pJex-fliC47-empty and (b) pJex-fliC47-cutinase, along with (c) the prototype genetic synthetic modular secretion construct of pJex-fliC47-cutinase. Fig. S6. Comparison of growth of truncated FT3SS secretion strains. Growth curves for all relevant strains. Fig. S7. The FliC secretion signal is required to enable secretion. Immunoblots of secreted and intracellular cutinase. Fig. S8. Comparison of the ‘’late’ FliC and ‘early’ secretion signals. Schematic of secretion constructs and immunoblots of secreted and intracellular cutinase. Fig. S9. Secretion of a range of substrates through the optimised secretion strain. Immunoblots of secreted protein alongside a protein standard. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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