Harold Tjalsma

Type I signal peptidases of Gram-positive bacteria (2004)

Jongbloed, Jan D H, Tjalsma, Harold, Dubois, Jean-Yves F, Bron, Sierd, ...

Proteins that are exported from the cytoplasm to the periplasm and outer membrane of Gram-negative bacteria, or the cell wall and growth medium of Gram-positive bacteria, are generally synthesized as...

Subcellular sites for bacterial protein export (2004)

Campo, Nathalie, Tjalsma, Harold, Buist, Girbe, Stepniak, Dariusz, Meijer, Michel, Veenhuis, Marten, ...

Most bacterial proteins destined to leave the cytoplasm are exported to extracellular compartments or imported into the cytoplasmic membrane via the highly conserved SecA-YEG pathway. In the present...

Signal peptidases of Bacillus subtilis. A functional analysis. (1999)

Tjalsma, Harold

A common feature in cells of all living organisms is the export of proteins from their site of synthesis, usually the cytoplasm, to other destinations either inside or outside the cell. To achieve...

Signal peptidases of Bacillus subtilis : a functional analysis / (1999)

Tjalsma, Harold.

Thesis (doctoral)--Rijksuniversiteit te Groningen, 1999.

Evaluation of Bottlenecks in the Late Stages of Protein Secretion in Bacillus subtilis

Bolhuis, Albert, Tjalsma, Harold, Smith, Hilde E., De Jong, Anne, Meima, Rob, Venema, Gerard, ...

Despite a high capacity for secretion of homologous proteins, the secretion of heterologous proteins by Bacillus subtilis is frequently inefficient. In the present studies, we have investigated and...

Subunit II of Bacillus subtilis Cytochrome c Oxidase Is a Lipoprotein

Bengtsson, Jenny, Tjalsma, Harold, Rivolta, Carlo, Hederstedt, Lars

The sequence of the N-terminal end of the deduced ctaC gene product of Bacillus species has the features of a bacterial lipoprotein. CtaC is the subunit II of cytochrome caa3, which is a cytochrome c...

The Plasmid-Encoded Signal Peptidase SipP Can Functionally Replace the Major Signal Peptidases SipS and SipT of Bacillus subtilis

Tjalsma, Harold, Van Den Dolder, Juliëtte, Meijer, Wilfried J. J., Venema, Gerard, Bron, Sierd, Van Dijl, Jan Maarten

The gram-positive eubacterium Bacillus subtilis is the organism with the largest number of paralogous type I signal peptidases (SPases) known. These are specified both by chromosomal and...

Signal Peptide-Dependent Protein Transport in Bacillus subtilis: a Genome-Based Survey of the Secretome

Tjalsma, Harold, Bolhuis, Albert, Jongbloed, Jan D. H., Bron, Sierd, Van Dijl, Jan Maarten

One of the most salient features of Bacillus subtilis and related bacilli is their natural capacity to secrete a variety of proteins into their environment, frequently to high concentrations. This...

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...

Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases

Tjalsma, Harold, Bolhuis, Albert, Van Roosmalen, Maarten L., Wiegert, Thomas, Schumann, Wolfgang, Broekhuizen, Cees P., ...

Approximately 47% of the genes of the Gram-positive bacterium Bacillus subtilis belong to paralogous gene families. The present studies were aimed at the functional analysis of the sip gene family of...

Proteomics of Protein Secretion by Bacillus subtilis: Separating the “Secrets” of the Secretome

Tjalsma, Harold, Antelmann, Haike, Jongbloed, Jan D.H., Braun, Peter G., Darmon, Elise, Dorenbos, Ronald, ...

Secretory proteins perform a variety of important “remote-control” functions for bacterial survival in the environment. The availability of complete genome sequences has allowed us to make...

Evaluation of Bottlenecks in the Late Stages of Protein Secretion in Bacillus subtilis

Bolhuis, Albert, Tjalsma, Harold, Smith, Hilde E., De Jong, Anne, Meima, Rob, Venema, Gerard, ...

Despite a high capacity for secretion of homologous proteins, the secretion of heterologous proteins by Bacillus subtilis is frequently inefficient. In the present studies, we have investigated and...

Subunit II of Bacillus subtilis Cytochrome c Oxidase Is a Lipoprotein

Bengtsson, Jenny, Tjalsma, Harold, Rivolta, Carlo, Hederstedt, Lars

The sequence of the N-terminal end of the deduced ctaC gene product of Bacillus species has the features of a bacterial lipoprotein. CtaC is the subunit II of cytochrome caa3, which is a cytochrome c...

The Plasmid-Encoded Signal Peptidase SipP Can Functionally Replace the Major Signal Peptidases SipS and SipT of Bacillus subtilis

Tjalsma, Harold, Van Den Dolder, Juliëtte, Meijer, Wilfried J. J., Venema, Gerard, Bron, Sierd, Van Dijl, Jan Maarten

The gram-positive eubacterium Bacillus subtilis is the organism with the largest number of paralogous type I signal peptidases (SPases) known. These are specified both by chromosomal and...

Signal Peptide-Dependent Protein Transport in Bacillus subtilis: a Genome-Based Survey of the Secretome

Tjalsma, Harold, Bolhuis, Albert, Jongbloed, Jan D. H., Bron, Sierd, Van Dijl, Jan Maarten

One of the most salient features of Bacillus subtilis and related bacilli is their natural capacity to secrete a variety of proteins into their environment, frequently to high concentrations. This...

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...

Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases

Tjalsma, Harold, Bolhuis, Albert, Van Roosmalen, Maarten L., Wiegert, Thomas, Schumann, Wolfgang, Broekhuizen, Cees P., ...

Approximately 47% of the genes of the Gram-positive bacterium Bacillus subtilis belong to paralogous gene families. The present studies were aimed at the functional analysis of the sip gene family of...

Proteomics of Protein Secretion by Bacillus subtilis: Separating the “Secrets” of the Secretome

Tjalsma, Harold, Antelmann, Haike, Jongbloed, Jan D.H., Braun, Peter G., Darmon, Elise, Dorenbos, Ronald, ...

Secretory proteins perform a variety of important “remote-control” functions for bacterial survival in the environment. The availability of complete genome sequences has allowed us to make...

Advances in Quantitative Hepcidin Measurements by Time-of-Flight Mass Spectrometry

Swinkels, Dorine W., Girelli, Domenico, Laarakkers, Coby, Kroot, Joyce, Campostrini, Natascia, ...

Assays for the detection of the iron regulatory hormone hepcidin in plasma or urine have not yet been widely available, whereas quantitative comparisons between hepcidin levels in these different...