Juxtaposition of signal-peptide charge and core region hydrophobicity is critical for functional signal peptides (original) (raw)
Abstract.
In Escherichia coli, exported proteins are synthesized as precursors containing an amino-terminal signal peptide which directs transport through the translocase to the proper destination. We have constructed a series of signal peptide mutants, incorporating linker sequences of varying lengths between the amino-terminal charge and core region hydrophobicity, to examine the requirement for the juxtaposition of these two structural features in promoting protein transport. In vivo and in vitro analyses indicated that high transport efficiency via signal peptides with core regions of marginal hydrophobicity absolutely requires the proximity of sufficient charge.
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Authors and Affiliations
- Department of Molecular and Cell Biology, University of Connecticut, 75 North Eagleville Road, Storrs, CT 06269–3044, USA, , , , ,
Sharyn L. Rusch, Cynthia L. Mascolo, Maha O. Kebir & Debra A. Kendall
Authors
- Sharyn L. Rusch
- Cynthia L. Mascolo
- Maha O. Kebir
- Debra A. Kendall
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Rusch, S.L., Mascolo, C.L., Kebir, M.O. et al. Juxtaposition of signal-peptide charge and core region hydrophobicity is critical for functional signal peptides.Arch Microbiol 178, 306–310 (2002). https://doi.org/10.1007/s00203-002-0453-z
- Received: 25 March 2002
- Revised: 21 May 2002
- Accepted: 30 May 2002
- Issue date: October 2002
- DOI: https://doi.org/10.1007/s00203-002-0453-z