Literature DB >> 8801417

The endogenous Bacillus subtilis (natto) plasmids pTA1015 and pTA1040 contain signal peptidase-encoding genes: identification of a new structural module on cryptic plasmids.

W J Meijer1, A de Jong, G Bea, A Wisman, H Tjalsma, G Venema, S Bron, J M van Dijl.   

Abstract

Various strains of Bacillus subtilis (natto) contain small cryptic plasmids that replicate via the rolling-circle mechanism. Like plasmids from other Gram-positive bacteria, these plasmids are composed of several distinct structural modules. A new structural module was identified on the B. subtilis plasmids pTA1015 and pTA1040. It is composed of two genes: one specifies an unidentified protein with a putative signal peptide; and the other (sipP) specifies a functional type 1 signal peptidase (SPase). The homologous, but non-identical, sipP genes of the two plasmids are the first identified plasmid-specific SPase-encoding genes. With respect to structure and activity, the corresponding enzymes (denoted SipP) are highly similar to the chromosomally encoded SPase, SipP, of B. subtillis and several newly identified SPases of other bacilli. Our findings suggest that plasmid-encoded SPases have evolved because, of under certain conditions, SPase can be a limiting factor for protein secretion in B. subtilis.

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Year:  1995        PMID: 8801417     DOI: 10.1111/j.1365-2958.1995.mmi_17040621.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  19 in total

1.  Biofilm research uncovers a novel nonenzymatic signal peptidase function in Bacillus.

Authors:  Jan Maarten van Dijl
Journal:  J Bacteriol       Date:  2012-03-16       Impact factor: 3.490

Review 2.  Membrane proteases in the bacterial protein secretion and quality control pathway.

Authors:  Ross E Dalbey; Peng Wang; Jan Maarten van Dijl
Journal:  Microbiol Mol Biol Rev       Date:  2012-06       Impact factor: 11.056

3.  Relaxed specificity of the Bacillus subtilis TatAdCd translocase in Tat-dependent protein secretion.

Authors:  Robyn T Eijlander; Jan D H Jongbloed; Oscar P Kuipers
Journal:  J Bacteriol       Date:  2008-10-31       Impact factor: 3.490

Review 4.  The chemistry and enzymology of the type I signal peptidases.

Authors:  R E Dalbey; M O Lively; S Bron; J M van Dijl
Journal:  Protein Sci       Date:  1997-06       Impact factor: 6.725

Review 5.  Signal peptidase I: cleaving the way to mature proteins.

Authors:  Sarah M Auclair; Meera K Bhanu; Debra A Kendall
Journal:  Protein Sci       Date:  2011-11-22       Impact factor: 6.725

6.  Biochemical characterization of signal peptidase I from gram-positive Streptococcus pneumoniae.

Authors:  S B Peng; L Wang; J Moomaw; R B Peery; P M Sun; R B Johnson; J Lu; P Treadway; P L Skatrud; Q M Wang
Journal:  J Bacteriol       Date:  2001-01       Impact factor: 3.490

7.  The plasmid-encoded signal peptidase SipP can functionally replace the major signal peptidases SipS and SipT of Bacillus subtilis.

Authors:  H Tjalsma; J van den Dolder; W J Meijer; G Venema; S Bron; J M van Dijl
Journal:  J Bacteriol       Date:  1999-04       Impact factor: 3.490

8.  SipY Is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion.

Authors:  Arantxa Palacín; Víctor Parro; Nick Geukens; Jozef Anné; Rafael P Mellado
Journal:  J Bacteriol       Date:  2002-09       Impact factor: 3.490

9.  Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus.

Authors:  K M Cregg; I Wilding; M T Black
Journal:  J Bacteriol       Date:  1996-10       Impact factor: 3.490

10.  Immunity to the bacteriocin sublancin 168 Is determined by the SunI (YolF) protein of Bacillus subtilis.

Authors:  Jean-Yves F Dubois; Thijs R H M Kouwen; Anna K C Schurich; Carlos R Reis; Hendrik T Ensing; Erik N Trip; Jessica C Zweers; Jan Maarten van Dijl
Journal:  Antimicrob Agents Chemother       Date:  2008-12-01       Impact factor: 5.191

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