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Published on: August 9, 2022
Deletion analysis of the flagellum-specific secretion signal in Salmonella flagellin
Noémi Kovács1, Hajnalka Jankovics1, Ferenc Vonderviszt1
1Bio-Nanosystems Laboratory, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprém, Hungary.
Abstract:
The export signal recognized by the flagellum-specific export machinery is harbored within the highly conserved 26-47 segment of the disordered N-terminal part of Salmonella flagellin. In this work, we aimed to further localize the essential part of the export signal by deletion analysis and investigated how the length of the spacer segment preceding the signal affects export efficiency. Export signal variants were attached to a reporter protein, the CCP2 domain of human C1r protein, and export efficiency of the fusion constructs was studied. Our results suggest that almost any continuous oligopeptide of 8-10 residues within the 26-47 segment can efficiently direct flagellar export if preceded by a spacer segment of at least 15 amino acids without any specific sequential requirement.
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