Vesa P. Kontinen

Transcriptome analysis of the responses of Staphylococcus aureusto antimicrobial peptides and characterization of the roles of vraDEand vraSRin antimicrobial resistance (2009)

Pietiäinen, Milla, François, Patrice, Hyyryläinen, Hanne-Leena, Tangomo, Manuela, Sass, Vera, Sahl, Hans-Georg, ...

Abstract Background Understanding how pathogens respond to antimicrobial peptides, and how this compares to currently available antibiotics, is crucial for optimizing antimicrobial therapy....

Towards the development of Bacillus subtilisas a cell factory for membrane proteins and protein complexes (2008)

Zweers, Jessica C, Barák, Imrich, Becher, Dörte, Driessen, Arnold JM, Hecker, Michael, Kontinen, Vesa P, ...

Abstract Background The Gram-positive bacterium Bacillus subtilis is an important producer of high quality industrial enzymes and a few eukaryotic proteins. Most of these proteins are secreted into...

Towards the development of Bacillus subtilis as a cell factory for membrane proteins and protein complexes (2008)

Zweers, Jessica C., Barák, Imrich, Becher, Dörte, Driessen, Arnold J.M., Hecker, Michael, Kontinen, Vesa P., ...

Background: The Gram-positive bacterium Bacillus subtilis is an important producer of high quality industrial enzymes and a few eukaryotic proteins. Most of these proteins are secreted into the...

Roles of the Conserved Cytoplasmic Region and Non-Conserved Carboxy-Terminal Region of SecE in Escherichia coli Protein Translocase (1996)

Kontinen, Vesa P., Yamanaka, Miyuki, Nishiyama, Ken-ichi, Tokuda, Hajime

SecE, an essential membrane component of the Escherichia coli protein translocase, consists of 127 ami no acid residues. Only a part of the second putative cytoplasmic region comprising some 13...

Quantitation of the Capacity of the Secretion Apparatus and Requirement for PrsA in Growth and Secretion of α-Amylase in Bacillus subtilis

Vitikainen, Marika, Pummi, Tiina, Airaksinen, Ulla, Wahlström, Eva, Wu, Hongyan, Sarvas, Matti, ...

Regulated expression of AmyQ α-amylase of Bacillus amyloliquefaciens was used to examine the capacity of the protein secretion apparatus of B. subtilis. One B. subtilis cell was found to secrete...

ClpXP Protease Regulates the Signal Peptide Cleavage of Secretory Preproteins in Bacillus subtilis with a Mechanism Distinct from That of the Ecs ABC Transporter

Pummi, Tiina, Leskelä, Soile, Wahlström, Eva, Gerth, Ulf, Tjalsma, Harold, Hecker, Michael, ...

Identification and characterization of a suppressor mutation, sup-15, which partially restored secretion in the protein secretion-deficient Bacillus subtilis ecsA26 mutant, led us to discover a novel...

Quantitation of the Capacity of the Secretion Apparatus and Requirement for PrsA in Growth and Secretion of α-Amylase in Bacillus subtilis

Vitikainen, Marika, Pummi, Tiina, Airaksinen, Ulla, Wahlström, Eva, Wu, Hongyan, Sarvas, Matti, ...

Regulated expression of AmyQ α-amylase of Bacillus amyloliquefaciens was used to examine the capacity of the protein secretion apparatus of B. subtilis. One B. subtilis cell was found to secrete...

ClpXP Protease Regulates the Signal Peptide Cleavage of Secretory Preproteins in Bacillus subtilis with a Mechanism Distinct from That of the Ecs ABC Transporter

Pummi, Tiina, Leskelä, Soile, Wahlström, Eva, Gerth, Ulf, Tjalsma, Harold, Hecker, Michael, ...

Identification and characterization of a suppressor mutation, sup-15, which partially restored secretion in the protein secretion-deficient Bacillus subtilis ecsA26 mutant, led us to discover a novel...