Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery.
暂无分享,去创建一个
Zoya Ignatova | Volker Kasche | Z. Ignatova | A. Nurk | V. Kasche | Claudia Hörnle | Alan Nurk | C. Hörnle
[1] Ignatova,et al. The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli* , 2000, Enzyme and microbial technology.
[2] A. Economou. Bacterial protein translocase: a unique molecular machine with an army of substrates , 2000, FEBS letters.
[3] J. Weiner,et al. A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins , 1998, Cell.
[4] H. Sahm,et al. Expression of the Zymomonas mobilis gfo gene or NADP-containing glucose:fructose oxidoreductase (GFOR) in Escherichia coli. Formation of enzymatically active preGFOR but lack of processing into a stable periplasmic protein. , 1997, European journal of biochemistry.
[5] N Gottschlich,et al. Perfusible and non-perfusible supports with monoclonal antibodies for bioaffinity chromatography of Escherichia coli penicillin amidase within its pH stability range. , 1994, Journal of chromatography. A.
[6] B. Berks,et al. A naturally occurring bacterial Tat signal peptide lacking one of the ‘invariant’ arginine residues of the consensus targeting motif , 2001, FEBS letters.
[7] B. Berks,et al. The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting in Escherichia coli * , 2000, The Journal of Biological Chemistry.
[8] K. Cline,et al. The Thylakoid ΔpH-dependent Pathway Machinery Facilitates RR-independent N-Tail Protein Integration* , 2000, The Journal of Biological Chemistry.
[9] Gunnar von Heijne,et al. Competition between Sec‐ and TAT‐dependent protein translocation in Escherichia coli , 1999, The EMBO journal.
[10] B. Berks,et al. Overlapping functions of components of a bacterial Sec‐independent protein export pathway , 1998, The EMBO journal.
[11] K. Wilson,et al. Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft. , 2000, Journal of molecular biology.
[12] M. Bagdasarian,et al. A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants. , 1991, Gene.
[13] D. Klionsky,et al. How to get a folded protein across a membrane. , 1999, Trends in cell biology.
[14] G. von Heijne,et al. Domain structure of mitochondrial and chloroplast targeting peptides. , 1989, European journal of biochemistry.
[15] B. Berks. A common export pathway for proteins binding complex redox cofactors? , 1996, Molecular microbiology.
[16] A. Nurk,et al. Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli. , 1999, Biochimica et biophysica acta.
[17] G. Giordano,et al. A novel Sec‐independent periplasmic protein translocation pathway in Escherichia coli , 1998, The EMBO journal.