Comparison of Different Signal Sequences to Use for Periplasmic Over-Expression of Buforin I in Escherichia coli: An In Silico Study

作者: Sahar Roshanak , Farideh Tabatabaei Yazdi , Fakhri Shahidi , Ali Javadmanesh , Jebrail Movaffagh

DOI: 10.1007/S10989-020-10042-6

关键词: Periplasmic spaceExonucleaseEscherichia coliChemistrySignalStart codonSignal peptideUntranslated regionBiochemistryIn silico

摘要: Computational prediction of signal peptides is one the most important steps in genetic engineering experiments. The periplasmic expression cause reducing inherent destructive behavior Bofurin I against its host and also susceptibility to proteolytic degradation. In order predict best for Buforin E. coli, 103 sequences were retired from peptide databases. Since purpose this study was introduce optimal expression, first, sub-cellular localization site analyzed. Then, n, h, c regions peptide, probability physico-chemical features investigated. Base on results, MalE, hofQ, papK, ugpB, zraP, sfmC introduced as peptides. For increasing half-life mRNA stability exonuclease activity, secondary structures including Shine-Dalgarno, untranslated region ompA, start codon, Based total free energy pilot evaluated conformations, papK seemed more appropriate than rest obtained result can be used design constructs.

参考文章(53)
W.T. Godbey, Genes: The Blueprints for Proteins An Introduction to Biotechnology#R##N#The Science, Technology and Medical Applications. pp. 65- 105 ,(2015) , 10.1016/B978-1-907568-28-2.00004-6
Marc R. Wilkins, Elisabeth Gasteiger, Amos Bairoch, Jean-Charles Sanchez, Keith L. Williams, Ron D. Appel, Denis F. Hochstrasser, Protein identification and analysis tools in the ExPASy server Methods of Molecular Biology. ,vol. 112, pp. 531- 552 ,(1999) , 10.1385/1-59259-584-7:531
Khar Heng Choo, Tin Wee Tan, Shoba Ranganathan, SPdb--a signal peptide database. BMC Bioinformatics. ,vol. 6, pp. 249- 249 ,(2005) , 10.1186/1471-2105-6-249
Lukas Käll, Anders Krogh, Erik L.L Sonnhammer, A combined transmembrane topology and signal peptide prediction method. Journal of Molecular Biology. ,vol. 338, pp. 1027- 1036 ,(2004) , 10.1016/J.JMB.2004.03.016
A. Shokri, A. Sandén, G. Larsson, Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli Applied Microbiology and Biotechnology. ,vol. 60, pp. 654- 664 ,(2003) , 10.1007/S00253-002-1156-8
Kai Yu, Ling Lin, Sheng Hu, Jun Huang, Lehe Mei, C-terminal truncation of glutamate decarboxylase from Lactobacillus brevis CGMCC 1306 extends its activity toward near-neutral pH Enzyme and Microbial Technology. ,vol. 50, pp. 263- 269 ,(2012) , 10.1016/J.ENZMICTEC.2012.01.010
Tanya L. Johnson, Jan Abendroth, Wim G.J. Hol, Maria Sandkvist, Type II secretion: from structure to function. Fems Microbiology Letters. ,vol. 255, pp. 175- 186 ,(2006) , 10.1111/J.1574-6968.2006.00102.X
Daiki Takemori, Kenta Yoshino, Chisato Eba, Hideo Nakano, Yugo Iwasaki, Extracellular production of phospholipase A2 from Streptomyces violaceoruber by recombinant Escherichia coli. Protein Expression and Purification. ,vol. 81, pp. 145- 150 ,(2012) , 10.1016/J.PEP.2011.10.002
Matthias Freiherr von Roman, Anja Koller, Daniel von Rüden, Sonja Berensmeier, Improved extracellular expression and purification of recombinant Staphylococcus aureus protein A. Protein Expression and Purification. ,vol. 93, pp. 87- 92 ,(2014) , 10.1016/J.PEP.2013.10.013
Michael J. Hansen, Li-How Chen, Mariena L. S. Fejzo, Joel G. Beiasco, The ompA 5′ untranslated region impedes a major pathway for mRNA degradation in Escherichia coli Molecular Microbiology. ,vol. 12, pp. 707- 716 ,(1994) , 10.1111/J.1365-2958.1994.TB01058.X