The extracellular transport signal of the Vibrio cholerae endochitinase (ChiA) is a structural motif located between amino acids 75 and 555.

Journal of Bacteriology
Jason P Folster, Terry D Connell

Abstract

ChiA, an 88-kDa endochitinase encoded by the chiA gene of the gram-negative enteropathogen Vibrio cholerae, is secreted via the eps-encoded main terminal branch of the general secretory pathway (GSP), a mechanism which also transports cholera toxin. To localize the extracellular transport signal of ChiA that initiates transport of the protein through the GSP, a chimera comprised of ChiA fused at the N terminus with the maltose-binding protein (MalE) of Escherichia coli and fused at the C terminus with a 13-amino-acid epitope tag (E-tag) was expressed in strain 569B(chiA::Kan(r)), a chiA-deficient but secretion-competent mutant of V. cholerae. Fractionation studies revealed that blockage of the natural N terminus and C terminus of ChiA did not prevent secretion of the MalE-ChiA-E-tag chimera. To locate the amino acid sequences which encoded the transport signal, a series of truncations of ChiA were engineered. Secretion of the mutant polypeptides was curtailed only when ChiA was deleted from the N terminus beyond amino acid position 75 or from the C terminus beyond amino acid 555. A mutant ChiA comprised of only those amino acids was secreted by wild-type V. cholerae but not by an epsD mutant, establishing that amino acids 75 to...Continue Reading

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Citations

Apr 3, 2012·Nature Reviews. Microbiology·Konstantin V KorotkovWim G J Hol
Feb 5, 2008·Journal of Molecular Biology·Marissa E YanezWim G J Hol
Nov 12, 2015·Biochemistry. Biokhimii︠a︡·E Yu MarkovS V Balakhonov
May 10, 2017·Molecular Microbiology·Jenny-Lee ThomassinOlivera Francetic

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