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SepL resembles an aberrant effector in binding to a class 1 Type III secretion chaperone and carrying an N-Terminal secretion signal
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Younis, R., Bingle, L. E. H., Rollauer, S., Munera, D., Busby, S. J., Johnson, S., Deane, J. E., Lea, S. M., Frankel, G. and Pallen, Mark J. (2010) SepL resembles an aberrant effector in binding to a class 1 Type III secretion chaperone and carrying an N-Terminal secretion signal. Journal of Bacteriology, Volume 192 (Number 22). pp. 6093-6098. doi:10.1128/JB.00760-10
An open access version can be found in:
Official URL: http://dx.doi.org/10.1128/JB.00760-10
Abstract
Here we show that the type III secretion gatekeeper protein SepL resembles an aberrant effector protein in binding to a class 1 type III secretion chaperone (Orf12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.
| Item Type: | Journal Article | ||||
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| Divisions: | Faculty of Medicine > Warwick Medical School > Biomedical Sciences > Microbiology & Infection Faculty of Medicine > Warwick Medical School |
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| Journal or Publication Title: | Journal of Bacteriology | ||||
| Publisher: | American Society for Microbiology | ||||
| ISSN: | 0021-9193 | ||||
| Official Date: | 2010 | ||||
| Dates: |
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| Volume: | Volume 192 | ||||
| Number: | Number 22 | ||||
| Page Range: | pp. 6093-6098 | ||||
| DOI: | 10.1128/JB.00760-10 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Open Access | ||||
| Open Access Version: |
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