Identity Determinants of the Translocation Signal for a Type 1 Secretion System.
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Authors
Spitz, Olivia
Erenburg, Isabelle N
Kanonenberg, Kerstin
Peherstorfer, Sandra
Lenders, Michael HH
Reiners, Jens
Ma, Miao
Smits, Sander HJ
Schmitt, Lutz
Publication Date
2021Journal Title
Front Physiol
ISSN
1664-042X
Publisher
Frontiers Media
Type
Article
This Version
AM
Metadata
Show full item recordCitation
Spitz, O., Erenburg, I. N., Kanonenberg, K., Peherstorfer, S., Lenders, M. H., Reiners, J., Ma, M., et al. (2021). Identity Determinants of the Translocation Signal for a Type 1 Secretion System.. Front Physiol https://doi.org/10.3389/fphys.2021.804646
Abstract
The toxin hemolysin A was first identified in uropathogenic E. coli strains and shown to be secreted in a one-step mechanism by a dedicated secretion machinery. This machinery, which belongs to the Type I secretion system family of the Gram-negative bacteria, is composed of the outer membrane protein TolC, the membrane fusion protein HlyD and the ABC transporter HlyB. The N-terminal domain of HlyA represents the toxin which is followed by a RTX (Repeats in Toxins) domain harboring nonapeptide repeat sequences and the secretion signal at the extreme C-terminus. This secretion signal, which is necessary and sufficient for secretion, does not appear to require a defined sequence, and the nature of the encoded signal remains unknown. Here, we have combined structure prediction based on the AlphaFold algorithm together with functional and in silico data to examine the role of secondary structure in secretion. Based on the presented data, a C-terminal, amphipathic helix is proposed between residues 975 and 987 that plays an essential role in the early steps of the secretion process.
Sponsorship
ERC
Funder references
European Research Council (742210)
Identifiers
External DOI: https://doi.org/10.3389/fphys.2021.804646
This record's URL: https://www.repository.cam.ac.uk/handle/1810/332731
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