HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tjalsma, H. Articles by van Dijl, J. M. Search for Related Content PubMed PubMed Citation Articles by Tjalsma, H. Articles by van Dijl, J. M. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 3, 1698-1707, January 15, 1999

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 -AMYLASE, A NON-LIPOPROTEIN

Harold Tjalsma, Vesa P. Kontinen^¶, Zoltán Prágai^**, Hongyan Wu^¶, Rob Meima, Gerard Venema, Sierd Bron, Matti Sarvas^¶, and Jan Maarten van Dijl^§§

From the  Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands, the ^¶ Vaccine Development Laboratory, National Public Health Institute, Mannerheimintie 166, SF-00300 Helsinki, Finland, the ^** Department of Microbiology, The Medical School, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom, and the ^§§ Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands

Computer-assisted analyses indicate that Bacillus subtilis contains approximately 300 genes for exported proteins with an amino-terminal signal peptide. About 114 of these are lipoproteins, which are retained in the cytoplasmic membrane. We have investigated the importance of lipoprotein processing by signal peptidase II (SPase II) for cellular homeostasis, using cells lacking SPase II. The results show that lipoprotein processing is important for cell viability at low and high temperatures, suggesting that lipoproteins are essential for growth under these conditions. Although certain lipoproteins are required for the development of genetic competence, sporulation, and germination, these developmental processes were not affected in the absence of SPase II. Cells lacking SPase II accumulated lipid-modified precursor and mature-like forms of PrsA, a folding catalyst for secreted proteins. These forms of PrsA seem to have a reduced activity, as the secretion of -amylase was strongly impaired. Unexpectedly, type I signal peptidases, which process secretory preproteins, were not involved in alternative amino-terminal processing of pre-PrsA in the absence of SPase II. In conclusion, processing of lipoproteins by SPase II in B. subtilis is not strictly required for lipoprotein function, which is surprising as lipoproteins and type II SPases seem to be conserved in all eubacteria.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				M. Schmaler, N. J. Jann, F. Ferracin, L. Z. Landolt, L. Biswas, F. Gotz, and R. Landmann Lipoproteins in Staphylococcus aureus Mediate Inflammation by TLR2 and Iron-Dependent Growth In Vivo J. Immunol., June 1, 2009; 182(11): 7110 - 7118. [Abstract] [Full Text] [PDF]

				E. L. Denham, P. N. Ward, and J. A. Leigh In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp Microbiology, January 1, 2009; 155(1): 134 - 141. [Abstract] [Full Text] [PDF]

				P. L. Pelczar and P. Setlow Localization of the Germination Protein GerD to the Inner Membrane in Bacillus subtilis Spores J. Bacteriol., August 15, 2008; 190(16): 5635 - 5641. [Abstract] [Full Text] [PDF]

				E. L. Denham, P. N. Ward, and J. A. Leigh Lipoprotein Signal Peptides Are Processed by Lsp and Eep of Streptococcus uberis J. Bacteriol., July 1, 2008; 190(13): 4641 - 4647. [Abstract] [Full Text] [PDF]

				M. Baumgartner, U. Karst, B. Gerstel, M. Loessner, J. Wehland, and L. Jansch Inactivation of Lgt Allows Systematic Characterization of Lipoproteins from Listeria monocytogenes J. Bacteriol., January 15, 2007; 189(2): 313 - 324. [Abstract] [Full Text] [PDF]

				A. Hamilton, C. Robinson, I. C. Sutcliffe, J. Slater, D. J. Maskell, N. Davis-Poynter, K. Smith, A. Waller, and D. J. Harrington Mutation of the Maturase Lipoprotein Attenuates the Virulence of Streptococcus equi to a Greater Extent than Does Loss of General Lipoprotein Lipidation Infect. Immun., December 1, 2006; 74(12): 6907 - 6919. [Abstract] [Full Text] [PDF]

				M. I. Hutchings, H.-J. Hong, E. Leibovitz, I. C. Sutcliffe, and M. J. Buttner The {sigma}E Cell Envelope Stress Response of Streptomyces coelicolor Is Influenced by a Novel Lipoprotein, CseA. J. Bacteriol., October 1, 2006; 188(20): 7222 - 7229. [Abstract] [Full Text] [PDF]

				M. J. J. B. Sibbald, A. K. Ziebandt, S. Engelmann, M. Hecker, A. de Jong, H. J. M. Harmsen, G. C. Raangs, I. Stokroos, J. P. Arends, J. Y. F. Dubois, et al. Mapping the Pathways to Staphylococcal Pathogenesis by Comparative Secretomics Microbiol. Mol. Biol. Rev., September 1, 2006; 70(3): 755 - 788. [Abstract] [Full Text] [PDF]

				A. P. Bhavsar, R. Truant, and E. D. Brown The TagB Protein in Bacillus subtilis 168 Is an Intracellular Peripheral Membrane Protein That Can Incorporate Glycerol Phosphate onto a Membrane-bound Acceptor in Vitro J. Biol. Chem., November 4, 2005; 280(44): 36691 - 36700. [Abstract] [Full Text] [PDF]

				T. Igarashi and P. Setlow Interaction between Individual Protein Components of the GerA and GerB Nutrient Receptors That Trigger Germination of Bacillus subtilis Spores J. Bacteriol., April 1, 2005; 187(7): 2513 - 2518. [Abstract] [Full Text] [PDF]

				T. Stein, S. Heinzmann, S. Dusterhus, S. Borchert, and K.-D. Entian Expression and Functional Analysis of the Subtilin Immunity Genes spaIFEG in the Subtilin-Sensitive Host Bacillus subtilis MO1099 J. Bacteriol., February 1, 2005; 187(3): 822 - 828. [Abstract] [Full Text] [PDF]

				C. Robichon, D. Vidal-Ingigliardi, and A. P. Pugsley Depletion of Apolipoprotein N-Acyltransferase Causes Mislocalization of Outer Membrane Lipoproteins in Escherichia coli J. Biol. Chem., January 14, 2005; 280(2): 974 - 983. [Abstract] [Full Text] [PDF]

				H. Tjalsma, H. Antelmann, J. D.H. Jongbloed, P. G. Braun, E. Darmon, R. Dorenbos, J.-Y. F. Dubois, H. Westers, G. Zanen, W. J. Quax, et al. Proteomics of Protein Secretion by Bacillus subtilis: Separating the "Secrets" of the Secretome Microbiol. Mol. Biol. Rev., June 1, 2004; 68(2): 207 - 233. [Abstract] [Full Text] [PDF]

				T. Igarashi, B. Setlow, M. Paidhungat, and P. Setlow Effects of a gerF (lgt) Mutation on the Germination of Spores of Bacillus subtilis J. Bacteriol., May 15, 2004; 186(10): 2984 - 2991. [Abstract] [Full Text] [PDF]

				H. Reglier-Poupet, C. Frehel, I. Dubail, J.-L. Beretti, P. Berche, A. Charbit, and C. Raynaud Maturation of Lipoproteins by Type II Signal Peptidase Is Required for Phagosomal Escape of Listeria monocytogenes J. Biol. Chem., December 5, 2003; 278(49): 49469 - 49477. [Abstract] [Full Text] [PDF]

				S. Y. M. Ng and K. F. Jarrell Cloning and Characterization of Archaeal Type I Signal Peptidase from Methanococcus voltae J. Bacteriol., October 15, 2003; 185(20): 5936 - 5942. [Abstract] [Full Text] [PDF]

				A. de Greeff, A. Hamilton, I. C. Sutcliffe, H. Buys, L. van Alphen, and H. E. Smith Lipoprotein signal peptidase of Streptococcus suis serotype 2 Microbiology, June 1, 2003; 149(6): 1399 - 1407. [Abstract] [Full Text] [PDF]

				H. Tjalsma, S. Bron, and J. M. van Dijl Complementary Impact of Paralogous Oxa1-like Proteins of Bacillus subtilis on Post-translocational Stages in Protein Secretion J. Biol. Chem., April 25, 2003; 278(18): 15622 - 15632. [Abstract] [Full Text] [PDF]

				R. Venema, H. Tjalsma, J. M. van Dijl, A. de Jong, K. Leenhouts, G. Buist, and G. Venema Active Lipoprotein Precursors in the Gram-positive Eubacterium Lactococcus lactis J. Biol. Chem., April 18, 2003; 278(17): 14739 - 14746. [Abstract] [Full Text] [PDF]

				A. K. Dunn, A. K. Klimowicz, and J. Handelsman Use of a Promoter Trap To Identify Bacillus cereus Genes Regulated by Tomato Seed Exudate and a Rhizosphere Resident, Pseudomonas aureofaciens Appl. Envir. Microbiol., February 1, 2003; 69(2): 1197 - 1205. [Abstract] [Full Text] [PDF]

				T. Stein, S. Heinzmann, I. Solovieva, and K.-D. Entian Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis J. Biol. Chem., January 3, 2003; 278(1): 89 - 94. [Abstract] [Full Text] [PDF]

				J. D. H. Jongbloed, H. Antelmann, M. Hecker, R. Nijland, S. Bron, U. Airaksinen, F. Pries, W. J. Quax, J. M. van Dijl, and P. G. Braun Selective Contribution of the Twin-Arginine Translocation Pathway to Protein Secretion in Bacillus subtilis J. Biol. Chem., November 8, 2002; 277(46): 44068 - 44078. [Abstract] [Full Text] [PDF]

				I. C. Sutcliffe and D. J. Harrington Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes Microbiology, July 1, 2002; 148(7): 2065 - 2077. [Abstract] [Full Text] [PDF]

				K. Masuda, S.-i. Matsuyama, and H. Tokuda Elucidation of the function of lipoprotein-sorting signals that determine membrane localization PNAS, May 28, 2002; 99(11): 7390 - 7395. [Abstract] [Full Text] [PDF]

				J. J. Sakamoto, M. Sasaki, and T. Tsuchido Purification and Characterization of a Bacillus subtilis 168 Nuclease, YokF, Involved in Chromosomal DNA Degradation and Cell Death Caused by Thermal Shock Treatments J. Biol. Chem., December 7, 2001; 276(50): 47046 - 47051. [Abstract] [Full Text] [PDF]

				H. Antelmann, H. Tjalsma, B. Voigt, S. Ohlmeier, S. Bron, J. M. van Dijl, and M. Hecker A Proteomic View on Genome-Based Signal Peptide Predictions Genome Res., September 1, 2001; 11(9): 1484 - 1502. [Abstract] [Full Text] [PDF]

				M. Vitikainen, T. Pummi, U. Airaksinen, E. Wahlström, H. Wu, M. Sarvas, and V. P. Kontinen Quantitation of the Capacity of the Secretion Apparatus and Requirement for PrsA in Growth and Secretion of {alpha}-Amylase in Bacillus subtilis J. Bacteriol., March 15, 2001; 183(6): 1881 - 1890. [Abstract] [Full Text]

				M. Nishiguchi, M. Matsumoto, T. Takao, M. Hoshino, Y. Shimonishi, S. Tsuji, N. A. Begum, O. Takeuchi, S. Akira, K. Toyoshima, et al. Mycoplasma fermentans Lipoprotein M161Ag-Induced Cell Activation Is Mediated by Toll-Like Receptor 2: Role of N-Terminal Hydrophobic Portion in its Multiple Functions J. Immunol., February 15, 2001; 166(4): 2610 - 2616. [Abstract] [Full Text] [PDF]

				K.-I. Yoshida, Y. Fujita, and S. D. Ehrlich An Operon for a Putative ATP-Binding Cassette Transport System Involved in Acetoin Utilization of Bacillus subtilis J. Bacteriol., October 1, 2000; 182(19): 5454 - 5461. [Abstract] [Full Text]

				H. Tjalsma, A. Bolhuis, J. D. H. Jongbloed, S. Bron, and J. M. van Dijl Signal Peptide-Dependent Protein Transport in Bacillus subtilis: a Genome-Based Survey of the Secretome Microbiol. Mol. Biol. Rev., September 1, 2000; 64(3): 515 - 547. [Abstract] [Full Text] [PDF]

				I. Hirose, K. Sano, I. Shioda, M. Kumano, K. Nakamura, and K. Yamane Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study Microbiology, January 1, 2000; 146(1): 65 - 75. [Abstract] [Full Text]

				H. Tjalsma, G. Zanen, G. Venema, S. Bron, and J. M. van Dijl The Potential Active Site of the Lipoprotein-specific (Type II) Signal Peptidase of Bacillus subtilis J. Biol. Chem., October 1, 1999; 274(40): 28191 - 28197. [Abstract] [Full Text] [PDF]

				A. Bolhuis, G. Venema, W. J. Quax, S. Bron, and J. M. van Dijl Functional Analysis of Paralogous Thiol-disulfide Oxidoreductases in Bacillus subtilis J. Biol. Chem., August 27, 1999; 274(35): 24531 - 24538. [Abstract] [Full Text] [PDF]

				A. Bolhuis, A. Matzen, H.-L. Hyyrylainen, V. P. Kontinen, R. Meima, J. Chapuis, G. Venema, S. Bron, R. Freudl, and J. M. van Dijl Signal Peptide Peptidase- and ClpP-like Proteins of Bacillus subtilis Required for Efficient Translocation and Processing of Secretory Proteins J. Biol. Chem., August 27, 1999; 274(35): 24585 - 24592. [Abstract] [Full Text] [PDF]

				J. D. H. Jongbloed, U. Martin, H. Antelmann, M. Hecker, H. Tjalsma, G. Venema, S. Bron, J. M. van Dijl, and J. Muller TatC Is a Specificity Determinant for Protein Secretion via the Twin-arginine Translocation Pathway J. Biol. Chem., December 22, 2000; 275(52): 41350 - 41357. [Abstract] [Full Text] [PDF]