A positive residue in the hydrophobic core of the Escherichia coli lipoprotein signal peptide suppresses the secretion defect caused by an acidic amino terminus.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference22 articles.
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1. Site-saturation mutagenesis of mutant l-asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase;Journal of Industrial Microbiology and Biotechnology;2017-12-01
2. Export of a hyperexpressed mammalian globular cytochrome b5precursor inEscherichia coliis dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond;Protein Science;2010-05-05
3. Do more complex organisms have a greater proportion of membrane proteins in their genomes?;Proteins: Structure, Function, and Genetics;2000-06-01
4. Effect of alteration of charged residues at the N termini of signal peptides on protein export in Bacillus subtilis;Journal of Bacteriology;1994-09
5. Signal peptides: exquisitely designed transport promoters;Molecular Microbiology;1994-09
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