Authors:
Tjalsma, H
Bolhuis, A
Jongbloed, JDH
Bron, S
van Dijl, JM
Citation: H. Tjalsma et al., Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome, MICRO M B R, 64(3), 2000, pp. 515
Authors:
Jongbloed, JDH
Martin, U
Antelmann, H
Hecker, M
Tjalsma, H
Venema, G
Bron, S
van Dijl, JM
Muller, J
Citation: Jdh. Jongbloed et al., TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway, J BIOL CHEM, 275(52), 2000, pp. 41350-41357
Authors:
Tjalsma, H
Stover, AG
Driks, A
Venema, G
Bron, S
van Dijl, JM
Citation: H. Tjalsma et al., Conserved serine and histidine residues are critical for activity of the ER-type signal peptidase SipW of Bacillus subtilis, J BIOL CHEM, 275(33), 2000, pp. 25102-25108
Authors:
Bolhuis, A
Tjalsma, H
Smith, HE
de Jong, A
Meima, R
Venema, G
Bron, S
van Dijl, JM
Citation: A. Bolhuis et al., Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilis, APPL ENVIR, 65(7), 1999, pp. 2934-2941
Authors:
Tjalsma, H
Zanen, G
Venema, G
Bron, S
van Dijl, JM
Citation: H. Tjalsma et al., The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis, J BIOL CHEM, 274(40), 1999, pp. 28191-28197
Authors:
Tjalsma, H
Kontinen, VP
Pragai, Z
Wu, HY
Meima, R
Venema, G
Bron, S
Sarvas, M
van Dijl, JM
Citation: H. Tjalsma et al., The role of lipoprotein processing by signal peptidase II in the Gram-positive eubacterium Bacillus subtilis - Signal peptidase II is required for the efficient secretion of alpha-amylase, a non-lipoprotein, J BIOL CHEM, 274(3), 1999, pp. 1698-1707
Authors:
Bolhuis, A
Tjalsma, H
Stephenson, K
Harwood, CR
Venema, G
Bron, S
van Dijl, JM
Citation: A. Bolhuis et al., Different mechanisms for thermal inactivation of Bacillus subtilis signal peptidase mutants, J BIOL CHEM, 274(22), 1999, pp. 15865-15868
Authors:
Tjalsma, H
van den Dolder, J
Meijer, WJJ
Venema, G
Bron, S
van Dijl, JM
Citation: H. Tjalsma et al., The plasmid-encoded signal peptidase SipP can functionally replace the major signal peptidases SipS and SipT of Bacillus subtilis, J BACT, 181(8), 1999, pp. 2448-2454
Authors:
Schacht, S
Van Mellaert, L
Lammertyn, E
Tjalsma, H
Van Dijl, JM
Bron, S
Anne, J
Citation: S. Schacht et al., The Sip(Sli) gene of Streptomyces lividans TK24 specifies an unusual signal peptidase with a putative C-terminal transmembrane anchor, DNA SEQ, 9(2), 1998, pp. 79-88