Optimization of a bacillus sp signal peptide for improved recombinant protein secretion and cell viability in escherichia coli is there an optimal signal peptide design?

Bioengineered

Volumn 3, Issue 6, 2012, Pages 334-338

  Low, Kheng Oon ^a   Jonet, Mohd Anuar ^a   Ismail, Noor Faizah ^a   Illias, Rosli Md ^a  

^a UNIVERSITI TEKNOLOGI MALAYSIA   (Malaysia)

Author keywords

Cell lysis; Escherichia coli; Helix breaking residue; Protein secretion; Signal peptide

Indexed keywords

G1 SIGNAL PEPTIDE; HELIX LOOP HELIX PROTEIN; PELB PROTEIN; RECOMBINANT PROTEIN; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS; CELL VIABILITY; ESCHERICHIA COLI; NONHUMAN; PROCESS OPTIMIZATION; PROTEIN DOMAIN; PROTEIN SECRETION; PROTEIN TARGETING; SECRETORY PATHWAY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; ESCHERICHIA COLI; MICROBIAL VIABILITY; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PERIPLASM; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT PROTEINS; RESEARCH DESIGN;

BACILLUS SP.; ESCHERICHIA COLI;

EID: 84868558504     PISSN: 19491018     EISSN: 19491026     Source Type: Journal    
DOI: None     Document Type: Article

References (17)

1. Yoon SH, Kim SK, Kim JF. Secretory production of recombinant proteins in Escherichia coli. Recent Pat Biotechnol 2010; 4:23-9; PMID:20201800; http:// dx.doi.org/10.2174/187220810790069550.
2. Mergulhão FJM, Summers DK, Monteiro GA. Recombinant protein secretion in Escherichia coli. Biotechnol Adv 2005; 23:177-202; PMID:15763404; http://dx.doi.org/10.1016/j.biotechadv.2004.11.003.
3. Choi JH, Lee SY. Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 2004; 64:625-35; PMID:14966662; http://dx.doi.org/10.1007/s00253- 004-1559-9.
4. Ni Y, Chen R. Extracellular recombinant protein production from Escherichia coli. Biotechnol Lett 2009; 31:1661-70; PMID:19597765; http://dx.doi. org/10.1007/s10529-009-0077-3.
5. Fu ZB, Ng KL, Lam TL, Wong WK. Cell death caused by hyper-expression of a secretory exoglucanase in Escherichia coli. Protein Expr Purif 2005; 42:67- 77; PMID:15882948; http://dx.doi.org/10.1016/j. pep.2005.03.029.
6. von Heijne G, Abrahmsén L. Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts. FEBS Lett 1989; 244:439- 46; PMID:2646153; http://dx.doi.org/10.1016/0014- 5793(89)80579-4.
7. Ismail NF, Hamdan S, Mahadi NM, Murad AM, Rabu A, Bakar FD, et al. A mutant L-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of Escherichia coli. Biotechnol Lett 2011; 33:999-1005; PMID:21234789; http://dx.doi.org/10.1007/s10529- 011-0517-8.
8. Jonet MA, Mahadi NM, Murad AM, Rabu A, Bakar FD, Rahim RA, et al. Optimization of a heterologous signal peptide by site-directed mutagenesis for improved secretion of recombinant proteins in Escherichia coli. J Mol Microbiol Biotechnol 2012; 22:48-58; PMID:22456489; http://dx.doi. org/10.1159/000336524.
9. Choi JH, Jeong KJ, Kim SC, Lee SY. Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence. Appl Microbiol Biotechnol 2000; 53:640-5; PMID:10919319; http:// dx.doi.org/10.1007/s002530000334.
10. Low KO, Mahadi NM, Rahim RA, Rabu A, Abu Bakar FD, Murad AM, et al. An effective extracellular protein secretion by an ABC transporter system in Escherichia coli: statistical modeling and optimization of cyclodextrin glucanotransferase secretory production. J Ind Microbiol Biotechnol 2011; 38:1587-97; PMID:21336875; http://dx.doi.org/10.1007/s10295- 011-0949-0.
11. Villa R, Lotti M, Gatti-Lafranconi P. Components of the E. coli envelope are affected by and can react to protein over-production in the cytoplasm. Microb Cell Fact 2009; 8:32; PMID:19500339; http://dx.doi. org/10.1186/1475-2859-8-32.
12. Li Z, Gu Z, Wang M, Du G, Wu J, Chen J. Delayed supplementation of glycine enhances extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli. Appl Microbiol Biotechnol 2010; 85:553-61; PMID:19655137; http:// dx.doi.org/10.1007/s00253-009-2157-7.
13. Lemberg MK, Bland FA, Weihofen A, Braud VM, Martoglio B. Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes. J Immunol 2001; 167:6441-6; PMID:11714810.
14. Lemberg MK, Martoglio B. Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis. Mol Cell 2002; 10:735-44; PMID:12419218; http:// dx.doi.org/10.1016/S1097-2765(02)00655-X.
15. Zwizinski C, Wickner W. Purification and characterization of leader (signal) peptidase from Escherichia coli. J Biol Chem 1980; 255:7973-7; PMID:6995457.
16. Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004; 32:1792-7; PMID:15034147; http://dx.doi. org/10.1093/nar/gkh340.
17. Crooks GE, Hon G, Chandonia JM, Brenner SE. WebLogo: a sequence logo generator. Genome Res 2004; 14:1188-90; PMID:15173120; http://dx.doi. org/10.1101/gr.849004.