Literature DB >> 1587474

Modular expression and secretion vectors for Bacillus subtilis.

V Nagarajan1, H Albertson, M Chen, J Ribbe.   

Abstract

A modular vector system has been developed for the extracellular production of heterologous proteins in Bacillus subtilis. This modular vector system consists of four secretion vectors which are based upon the genes encoding the Bacillus amyloliquefaciens extracellular alkaline protease, neutral protease, barnase and levansucrase. The modular vectors contain compatible restriction sites downstream from the signal peptide-coding region. Three reporter proteins (staphylococcal protein A, levansucrase and Escherichia coli alkaline phosphatase) that offer complementary advantages for cloning, genetic manipulations and media optimization have been fused to the various signal peptides. These secretion vectors function in E. coli and hence can be used to compare the mechanisms of protein secretion in E. coli and B. subtilis.

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Year:  1992        PMID: 1587474     DOI: 10.1016/0378-1119(92)90717-4

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  11 in total

1.  Chloramphenicol acetyltransferase, a cytoplasmic protein is incompatible for export from Bacillus subtilis.

Authors:  M W Chen; V Nagarajan
Journal:  J Bacteriol       Date:  1993-09       Impact factor: 3.490

2.  Versatile expression and secretion vectors for Bacillus subtilis.

Authors:  Ulf Brockmeier; Marion Wendorff; Thorsten Eggert
Journal:  Curr Microbiol       Date:  2006-01-31       Impact factor: 2.188

3.  Use of transposon promoter-probe vectors in the metabolic engineering of the obligate methanotroph Methylomonas sp. strain 16a for enhanced C40 carotenoid synthesis.

Authors:  Pamela L Sharpe; Deana Dicosimo; Melissa D Bosak; Kyle Knoke; Luan Tao; Qiong Cheng; Rick W Ye
Journal:  Appl Environ Microbiol       Date:  2007-01-19       Impact factor: 4.792

4.  Escherichia coli signal peptides direct inefficient secretion of an outer membrane protein (OmpA) and periplasmic proteins (maltose-binding protein, ribose-binding protein, and alkaline phosphatase) in Bacillus subtilis.

Authors:  D N Collier
Journal:  J Bacteriol       Date:  1994-05       Impact factor: 3.490

5.  Effect of alteration of charged residues at the N termini of signal peptides on protein export in Bacillus subtilis.

Authors:  M Chen; V Nagarajan
Journal:  J Bacteriol       Date:  1994-09       Impact factor: 3.490

6.  SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membrane.

Authors:  P McNicholas; T Rajapandi; D Oliver
Journal:  J Bacteriol       Date:  1995-12       Impact factor: 3.490

7.  The roles of signal peptide and mature protein in RNase (barnase) export from Bacillus subtilis.

Authors:  M Chen; V Nagarajan
Journal:  Mol Gen Genet       Date:  1993-06

8.  Characterization of the secretion efficiency of a plant signal peptide in Bacillus subtilis.

Authors:  J Ribbe; V Nagarajan
Journal:  Mol Gen Genet       Date:  1992-11

9.  Secretion of streptavidin from Bacillus subtilis.

Authors:  V Nagarajan; R Ramaley; H Albertson; M Chen
Journal:  Appl Environ Microbiol       Date:  1993-11       Impact factor: 4.792

10.  Evaluation of the Staphylococcus aureus class C nonspecific acid phosphatase (SapS) as a reporter for gene expression and protein secretion in gram-negative and gram-positive bacteria.

Authors:  Erika du Plessis; Jacques Theron; Eldie Berger; Maureen Louw
Journal:  Appl Environ Microbiol       Date:  2007-09-28       Impact factor: 4.792

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