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D. Koshland, R. Sauer, D. Botstein (1982)
Diverse effects of mutations in the signal sequence on the secretion of β-lactamase in Salmonella typhimuriumCell, 30
P. Natale, T. Brüser, A. Driessen (2008)
Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane--distinct translocases and mechanisms.Biochimica et biophysica acta, 1778 9
M. Carrio, A. Villaverde (2002)
Construction and deconstruction of bacterial inclusion bodies.Journal of biotechnology, 96 1
(1989)
Molecu lar Cloning: A Laboratory Manual, New York: Cold Spring Harbor
P. Fekkes, A. Driessen (1999)
Protein Targeting to the Bacterial Cytoplasmic MembraneMicrobiology and Molecular Biology Reviews, 63
G. Georgiou, Laura Segatori (2005)
Preparative expression of secreted proteins in bacteria: status report and future prospects.Current opinion in biotechnology, 16 5
R. Dalbey, M. Lively, S. Bron, J. Dijl (1997)
The chemistry and enzymology of the type I signal peptidasesProtein Science, 6
J. Sambrook, E. Fritsch, T. Maniatis (2001)
Molecular Cloning: A Laboratory Manual
R. Dalbey, W. Wickner (1985)
Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane.The Journal of biological chemistry, 260 29
G. Heijne (1998)
Protein transport: Life and death of a signal peptideNature, 396
F. Mergulhão, D. Summers, G. Monteiro (2005)
Recombinant protein secretion in Escherichia coli.Biotechnology advances, 23 3
Y. Liao, Jen‐Chong Jeng, Chiu-Feng Wang, Sui-Chi Wang, Shu-Ting Chang (2004)
Removal of N‐terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidaseProtein Science, 13
U. Laemmli (1970)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 227
J. Choi, S. Lee (2004)
Secretory and extracellular production of recombinant proteins using Escherichia coliApplied Microbiology and Biotechnology, 64
A. Kuhn, W. Wickner (1985)
Conserved residues of the leader peptide are essential for cleavage by leader peptidase.The Journal of biological chemistry, 260 29
Enterotoxin A containing various leader sequences have been obtained by site-driven mutagenesis. Some of them were capable of providing the translocation of recombinant SEA to E. coli periplasmic space. Structure of C-region of the signal peptide is essential for intracellular protein location. Substitution of a more common to E. coli proproteins Ala-Ser-Ala for the authentic sequence of Val-Asn-Gly is the most important in recognition by signal peptidase type I.
Applied Biochemistry and Microbiology – Springer Journals
Published: Nov 12, 2010
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