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Article: Isolation and characterization of dominant mutations in the Bacillus subtilis stressosome components RsbR and RsbS.

Reeves, Adam / Haldenwang, W G

2007 Volume 189, Issue 5, Page(s) 1531–1541

Abstract: The general stress response of Bacillus subtilis is controlled by the activity state of the sigma(B) transcription factor. Physical stress is communicated to sigma(B) via a large-molecular-mass (>10(6)-Da) structure (the stressosome) formed by one or ... ...

Abstract	The general stress response of Bacillus subtilis is controlled by the activity state of the sigma(B) transcription factor. Physical stress is communicated to sigma(B) via a large-molecular-mass (>10(6)-Da) structure (the stressosome) formed by one or more members of a family of homologous proteins (RsbR, YkoB, YojH, YqhA). The positive regulator (RsbT) of the sigma(B) stress induction pathway is incorporated into the complex bound to an inhibitor protein (RsbS). Exposure to stress empowers an RsbT-dependent phosphorylation of RsbR and RsbS, with the subsequent release of RsbT to activate downstream processes. The mechanism by which stress initiates these reactions is unknown. In an attempt to identify changes in stressosome components that could lead to sigma(B) activation, a DNA segment encoding these proteins was mutagenized and placed into B. subtilis to create a merodiploid strain for these genes. Eight mutations that allowed heightened sigma(B) activity in the presence of their wild-type counterparts were isolated. Two of the mutations are missense changes in rsbR, and six are amino acid changes in rsbS. Additional experiments suggested that both of the rsbR mutations and three of the rsbS mutations likely enhance sigma(B) activity by elevating the level of RsbS phosphorylation. All of the mutations were found to be dominant over wild-type alleles only when they are cotranscribed within an rsbR rsbS rsbT operon. The data suggest that changes in RsbR can initiate the downstream events that lead to sigma(B) activation and that RsbR, RsbS, and RsbT likely interact with each other concomitantly with their synthesis.
MeSH term(s)	Alleles ; Amino Acid Sequence ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/physiology ; Molecular Sequence Data ; Mutation ; Phosphoproteins/genetics ; Phosphoproteins/physiology ; Phosphorylation ; Sigma Factor/physiology
Chemical Substances	Bacterial Proteins ; Phosphoproteins ; RsbR protein, Bacillus subtilis ; SigB protein, Bacteria ; Sigma Factor
Language	English
Publishing date	2007-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.01649-06
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Article: Contributions of ATP, GTP, and redox state to nutritional stress activation of the Bacillus subtilis sigmaB transcription factor.

Zhang, Shuyu / Haldenwang, W G

Journal of bacteriology

2005 Volume 187, Issue 22, Page(s) 7554–7560

Abstract: The general stress regulon of Bacillus subtilis is induced by activation of the sigma(B) transcription factor. sigma(B) activation occurs when one of two phosphatases responds to physical or nutritional stress to activate a positive sigma(B) regulator by ...

Abstract	The general stress regulon of Bacillus subtilis is induced by activation of the sigma(B) transcription factor. sigma(B) activation occurs when one of two phosphatases responds to physical or nutritional stress to activate a positive sigma(B) regulator by dephosphorylation. The signal that triggers the nutritional stress phosphatase (RsbP) is unknown; however, RsbP activation occurs under culture conditions (glucose/phosphate starvation, azide or decoyinine treatment) that reduce the cell's levels of ATP and/or GTP. Variances in nucleotide levels in these instances may be coincidental rather than causal. RsbP carries a domain (PAS) that in some regulatory systems can respond directly to changes in electron transport, proton motive force, or redox potential, changes that typically precede shifts in high-energy nucleotide levels. The current work uses Bacillus subtilis with mutations in the oxidative phosphorylation and purine nucleotide biosynthetic pathways in conjunction with metabolic inhibitors to better define the inducing signal for RsbP activation. The data argue that a drop in ATP, rather than changes in GTP, proton motive force, or redox state, is the key to triggering sigma(B) activation.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Guanosine Triphosphate/metabolism ; Mutation ; Oxidation-Reduction ; Oxidative Phosphorylation ; Phosphoric Monoester Hydrolases/physiology ; Purine Nucleotides/biosynthesis ; Sigma Factor/metabolism ; Transcription Factors/metabolism
Chemical Substances	Bacterial Proteins ; Purine Nucleotides ; SigB protein, Bacteria ; Sigma Factor ; Transcription Factors ; Guanosine Triphosphate (86-01-1) ; Adenosine Triphosphate (8L70Q75FXE) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
Language	English
Publishing date	2005-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.187.22.7554-7560.2005
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Article: The sigma factors of Bacillus subtilis.

Haldenwang, W G

Microbiological reviews

1995 Volume 59, Issue 1, Page(s) 1–30

Abstract: ... to intercellular cues. Other sigma factors (sigma B, sigma F, and sigma G) are inhibited by "anti-sigma factor ...

Abstract	The specificity of DNA-dependent RNA polymerase for target promotes is largely due to the replaceable sigma subunit that it carries. Multiple sigma proteins, each conferring a unique promoter preference on RNA polymerase, are likely to be present in all bacteria; however, their abundance and diversity have been best characterized in Bacillus subtilis, the bacterium in which multiple sigma factors were first discovered. The 10 sigma factors thus far identified in B. subtilis directly contribute to the bacterium's ability to control gene expression. These proteins are not merely necessary for the expression of those operons whose promoters they recognize; in many instances, their appearance within the cell is sufficient to activate these operons. This review describes the discovery of each of the known B. subtilis sigma factors, their characteristics, the regulons they direct, and the complex restrictions placed on their synthesis and activities. These controls include the anticipated transcriptional regulation that modulates the expression of the sigma factor structural genes but, in the case of several of the B. subtilis sigma factors, go beyond this, adding novel posttranslational restraints on sigma factor activity. Two of the sigma factors (sigma E and sigma K) are, for example, synthesized as inactive precursor proteins. Their activities are kept in check by "pro-protein" sequences which are cleaved from the precursor molecules in response to intercellular cues. Other sigma factors (sigma B, sigma F, and sigma G) are inhibited by "anti-sigma factor" proteins that sequester them into complexes which block their ability to form RNA polymerase holoenzymes. The anti-sigma factors are, in turn, opposed by additional proteins which participate in the sigma factors' release. The devices used to control sigma factor activity in B, subtilis may prove to be as widespread as multiple sigma factors themselves, providing ways of coupling sigma factor activation to environmental or physiological signals that cannot be readily joined to other regulatory mechanisms.
MeSH term(s)	Bacillus subtilis/chemistry ; Bacillus subtilis/physiology ; Gene Expression Regulation, Bacterial ; Sigma Factor/chemistry ; Sigma Factor/classification ; Sigma Factor/genetics ; Sigma Factor/isolation & purification ; Spores, Bacterial/chemistry
Chemical Substances	Sigma Factor
Language	English
Publishing date	1995-03
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	6864-0
ISSN	0146-0749
ISSN	0146-0749
DOI	10.1128/mr.59.1.1-30.1995
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Article: The influence of grain physicochemistry and biomass on hydraulic conductivity in sand-filled treatment wetlands

Welz, P.J / W. Mbasha / I. Smith / G. Holtman / G. Terblanche / M. Le Roes-Hill / R. Haldenwang

Ecological engineering. 2018 June, v. 116

2018

Abstract: The flow of effluent through treatment wetlands is influenced by the infrastructure set-up, the effluent character, the type of hydraulic flow, the mode of operation, the type of substrate, and the type and quantity of biomass. Current flow models have ... ...

Abstract	The flow of effluent through treatment wetlands is influenced by the infrastructure set-up, the effluent character, the type of hydraulic flow, the mode of operation, the type of substrate, and the type and quantity of biomass. Current flow models have not been well validated, and/or do not accurately account for biomass clogging. In this study, treatment wetlands containing Dune or River sand with similar particle size distributions exhibited significant disparities in achievable flow rates. To gain insight into this phenomenon, further investigations were conducted to compare: (i) sand particle characteristics (size, elemental and mineral composition, grain morphology), (ii) the relationships between mineral composition and shape of the sand particles, (iii) the hydraulic conductivity of the different sand types before and after inducement of biomass growth, and (iv) the measured hydraulic conductivities with those predicted using the fractional packing Kozeny-Carman model.Using automated scanning electron microscopy (QEMSCAN™) it was determined that the shape of the quartz particles of the River sand (98% quartz) and calcite particles of the Dune sand (81% quartz, 18% calcite) were less round and more angular than the quartz particles of the Dune sand, and that the River sand particles were conglomerate in nature and/or fractured. The hydraulic conductivities of the Dune and River sands were significantly different (0.284 and 0.015 mm s−1, respectively), and the hydraulic conductivity of the Dune sand decreased by 51% due to biomass accumulation. The fractional packing model overestimated the measured values.
Keywords	biomass production ; calcite ; ecosystem engineering ; hydraulic conductivity ; infrastructure ; mineral content ; models ; particle size distribution ; quartz ; rivers ; sand ; scanning electron microscopy ; wetlands
Language	English
Dates of publication	2018-06
Size	p. 21-30.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	1127407-4
ISSN	0925-8574
ISSN	0925-8574
DOI	10.1016/j.ecoleng.2018.02.017
Database	NAL-Catalogue (AGRICOLA)

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Article: Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes.

Zhang, Shuyu / Haldenwang, W G

Biochemical and biophysical research communications

2004 Volume 322, Issue 2, Page(s) 565–569

Abstract: Obg is a GTP-binding protein of Bacillus subtilis with essential, but undefined roles in the bacterium's growth, sporulation, and stress responses. Obg orthologs are widely conserved among both bacteria and eukaryotes. Gel filtration and affinity blot ... ...

Abstract	Obg is a GTP-binding protein of Bacillus subtilis with essential, but undefined roles in the bacterium's growth, sporulation, and stress responses. Obg orthologs are widely conserved among both bacteria and eukaryotes. Gel filtration and affinity blot assays have suggested that Obg may be ribosome-associated. In the current work, we continue an examination of the putative Obg:ribosome interaction. Velocity centrifugation analyses of crude B. subtilis extracts or purified Obg:ribosome mixtures suggest that Obg is initially ribosome-bound, but can separate from ribosomes during sedimentation in the absence of added nucleotides. Addition of either GTP, GDP or ATP to the gradient prolonged the Obg:ribosome association, while inclusion of a nonhydrolyzable GTP analog (5-guanylyl-imidodiphosphate) preserved it. The data strengthen the notion that Obg is a ribosome-associated protein, demonstrate that Obg's association with ribosomes is stabilized by GTP, and indicate that the ribosome-bound Obg can likely hydrolyze GTP and be released as a consequence.
MeSH term(s)	Bacillus subtilis/metabolism ; Bacterial Proteins/metabolism ; GTP-Binding Proteins/metabolism ; Guanosine Triphosphate/analogs & derivatives ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism ; Ribosomes/metabolism
Chemical Substances	Bacterial Proteins ; Obg GTP-binding protein, Bacteria ; Guanylyl Imidodiphosphate (34273-04-6) ; Guanosine Triphosphate (86-01-1) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2004-09-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2004.07.154
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Article: RelA is a component of the nutritional stress activation pathway of the Bacillus subtilis transcription factor sigma B.

Zhang, Shuyu / Haldenwang, W G

Journal of bacteriology

2003 Volume 185, Issue 19, Page(s) 5714–5721

Abstract: ... the activation of sigma(B) by physical stress (e.g., ethanol treatment) is not affected by the loss of RelA ...

Abstract	The general stress regulon of Bacillus subtilis is induced by the activation of the sigma(B) transcription factor. Activation of sigma(B) occurs when one of two phosphatases (RsbU and RsbP), each responding to a unique type of stress, actuates a positive regulator of sigma(B) by dephosphorylation. Nutritional stress triggers the RsbP phosphatase. The mechanism by which RsbP becomes active is unknown; however, its activation coincides with culture conditions that are likely to reduce the cell's levels of high-energy nucleotides. We now present evidence that RelA, a (p)ppGpp synthetase and the key enzyme of the stringent response, plays a role in nutritional stress activation of sigma(B). An insertion mutation that disrupts relA blocks the activation of sigma(B) in response to PO(4) or glucose limitation and inhibits the drop in ATP/GTP levels that normally accompanies sigma(B) induction under these conditions. In contrast, the activation of sigma(B) by physical stress (e.g., ethanol treatment) is not affected by the loss of RelA. RelA's role in sigma(B) activation appears to be distinct from its participation in the stringent response. Amino acid analogs which induce the stringent response and RelA-dependent (p)ppGpp synthesis do not trigger sigma(B) activity. In addition, neither a missense mutation in relA (relA240GE) nor a null mutation in rplK (rplK54), either of which is sufficient to inhibit the stringent response and RelA-dependent (p)ppGpp synthesis, fails to block sigma(B) activation by PO(4) or glucose limitation.
MeSH term(s)	Bacillus subtilis/enzymology ; Bacillus subtilis/growth & development ; Bacillus subtilis/physiology ; Bacterial Proteins/metabolism ; Culture Media ; Gene Expression Regulation, Bacterial ; Glucose/metabolism ; Ligases/genetics ; Ligases/metabolism ; Phosphates/metabolism ; Phosphoric Monoester Hydrolases ; Sigma Factor/metabolism ; Transcription Factors/metabolism
Chemical Substances	Bacterial Proteins ; Culture Media ; Phosphates ; SigB protein, Bacteria ; Sigma Factor ; Transcription Factors ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; RsbU protein, Bacillus subtilis (EC 3.1.3.3) ; Ligases (EC 6.-) ; guanosine 3',5'-polyphosphate synthetases (EC 6.-) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2003-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.185.19.5714-5721.2003
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Article: Tethering of the Bacillus subtilis sigma E proprotein to the cell membrane is necessary for its processing but insufficient for its stabilization.

Ju, Jingliang / Haldenwang, W G

Journal of bacteriology

2003 Volume 185, Issue 19, Page(s) 5897–5900

Abstract: sigma(E), a sporulation-specific transcription factor of Bacillus subtilis, is synthesized as an inactive proprotein with a 27-amino acid extension at its amino terminus. This "pro" sequence is removed by a developmentally regulated protease, but when ... ...

Abstract	sigma(E), a sporulation-specific transcription factor of Bacillus subtilis, is synthesized as an inactive proprotein with a 27-amino acid extension at its amino terminus. This "pro" sequence is removed by a developmentally regulated protease, but when present, it blocks sigma(E) activity, tethers sigma(E) to the bacterium's cytoplasmic membrane, and promotes sigma(E) stability. To investigate whether pro-sigma(E) processing and/or stabilization are tied to membrane sequestration, we used fluorescent protein fusions to examine the membrane binding of SigE variants. The results are consistent with membrane association as a prerequisite for pro-sigma(E) processing but not as a sufficient cause for the proprotein's stability.
MeSH term(s)	Amino Acid Sequence ; Bacillus subtilis/metabolism ; Bacillus subtilis/physiology ; Cell Membrane/metabolism ; Gene Expression Regulation, Bacterial ; Molecular Sequence Data ; Protein Precursors/chemistry ; Protein Precursors/genetics ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Protein Sorting Signals ; Sigma Factor/chemistry ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Spores, Bacterial ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Protein Precursors ; Protein Sorting Signals ; Sigma Factor ; Transcription Factors ; sporulation-specific sigma factors
Language	English
Publishing date	2003-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.185.19.5897-5900.2003
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Article: HrcA is a negative regulator of the dnaK and groESL operons of Streptococcus pyogenes.

Woodbury, Robyn / Haldenwang, W G

Biochemical and biophysical research communications

2003 Volume 302, Issue 4, Page(s) 722–727

Abstract: The genome of Streptococcus pyogenes, an important human pathogen, encodes homologs of the principal bacterial heat shock proteins DnaK and GroES, -EL, as well as HrcA, a negative regulator of dnaK and groESL expression in other Gram-positive bacteria. ... ...

Abstract	The genome of Streptococcus pyogenes, an important human pathogen, encodes homologs of the principal bacterial heat shock proteins DnaK and GroES, -EL, as well as HrcA, a negative regulator of dnaK and groESL expression in other Gram-positive bacteria. Using nuclease protection assays to measure dnaK/groESL mRNA abundance and a "non-polar" insertion to disrupt hrcA, we demonstrate that heat shock triggers a 4- to 8-fold increase in dnaK and groESL-specific mRNAs within 5 min of the temperature shift and that HrcA is a negative regulator of S. pyogenes dnaK/groESL mRNA abundance in unstressed S. pyogenes. Although the loss of HrcA elevated dnaK and groESL mRNA levels under non-heat shock conditions, the relative abundance of these RNAs increased further in heat shocked S. pyogenes, suggesting an additional element contributing to their synthesis or stability.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Chaperonins/genetics ; Chaperonins/metabolism ; DNA-Binding Proteins ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Operon ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Streptococcus pyogenes/genetics ; Streptococcus pyogenes/metabolism
Chemical Substances	Bacterial Proteins ; DNA-Binding Proteins ; Escherichia coli Proteins ; GroESL protein, Bacteria ; HSP70 Heat-Shock Proteins ; RNA, Bacterial ; RNA, Messenger ; Repressor Proteins ; Chaperonins (EC 3.6.1.-) ; dnaK protein, E coli (EC 3.6.1.-)
Language	English
Publishing date	2003-02-05
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/s0006-291x(03)00254-7
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Article ; Online: The growth-promoting and stress response activities of the Bacillus subtilis GTP binding protein Obg are separable by mutation.

Kuo, Shrin / Demeler, Borries / Haldenwang, W G

Journal of bacteriology

2008 Volume 190, Issue 20, Page(s) 6625–6635

Abstract: Bacillus subtilis Obg is a ribosome-associating GTP binding protein that is needed for growth, sporulation, and induction of the bacterium's general stress regulon (GSR). It is unclear whether the roles of Obg in sporulation and stress responsiveness are ...

Abstract	Bacillus subtilis Obg is a ribosome-associating GTP binding protein that is needed for growth, sporulation, and induction of the bacterium's general stress regulon (GSR). It is unclear whether the roles of Obg in sporulation and stress responsiveness are direct or a secondary effect of its growth-promoting functions. The present work addresses this question by an analysis of two obg alleles whose phenotypes argue for direct roles for Obg in each process. The first allele [obg(G92D)] encodes a missense change in the protein's highly conserved "obg fold" region. This mutation impairs cell growth and the ability of Obg to associate with ribosomes but fails to block sporulation or the induction of the GSR. The second obg mutation [obg(Delta22)] replaces the 22-amino-acid carboxy-terminal sequence of Obg with an alternative 26-amino-acid sequence. This Obg variant cofractionates with ribosomes and allows normal growth but blocks sporulation and impairs the induction of the GSR. Additional experiments revealed that the block on sporulation occurs early, preventing the activation of the essential sporulation transcription factor Spo0A, while inhibition of the GSR appears to involve a failure of the protein cascade that normally activates the GSR to effectively catalyze the reactions needed to activate the GSR transcription factor (sigma(B)).
MeSH term(s)	Adaptation, Physiological ; Amino Acid Sequence ; Artificial Gene Fusion ; Bacillus subtilis/genetics ; Bacillus subtilis/physiology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Genes, Reporter ; Models, Biological ; Molecular Sequence Data ; Mutation, Missense ; Protein Binding ; Ribosomes/metabolism ; Sequence Deletion ; Signal Transduction ; Spores, Bacterial/growth & development ; Two-Hybrid System Techniques ; beta-Galactosidase/biosynthesis ; beta-Galactosidase/genetics
Chemical Substances	Bacterial Proteins ; Obg GTP-binding protein, Bacteria ; spore-specific proteins, Bacillus ; beta-Galactosidase (EC 3.2.1.23) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2008-08-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00799-08
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Article: In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon.

Le Breton, Yoann / Mohapatra, Nrusingh Prasad / Haldenwang, W G

Applied and environmental microbiology

2006 Volume 72, Issue 1, Page(s) 327–333

Abstract: This report describes the construction and characterization of a mariner-based transposon system designed to be used in Bacillus subtilis, but potentially applicable to other gram-positive bacteria. Two pUC19-derived plasmids were created that contain ... ...

Abstract	This report describes the construction and characterization of a mariner-based transposon system designed to be used in Bacillus subtilis, but potentially applicable to other gram-positive bacteria. Two pUC19-derived plasmids were created that contain the mariner-Himar1 transposase gene, modified for expression in B. subtilis, under the control of either sigmaA- or sigmaB-dependent promoters. Both plasmids also contain a transposable element (TnYLB-1) consisting of a Kan r cassette bracketed by the Himar1-recognized inverse terminal repeats, as well as the temperature-sensitive replicon and Erm r gene of pE194ts. TnYLB-1 transposes into the B. subtilis chromosome with high frequency (10(-2)) from either plasmid. Southern hybridization analyses of 15 transposants and sequence analyses of the insertion sites of 10 of these are consistent with random transposition, requiring only a "TA" dinucleotide as the essential target in the recipient DNA. Two hundred transposants screened for sporulation proficiency and auxotrophy yielded five Spo- clones, three with insertions in known sporulation genes (kinA, spoVT, and yqfD) and two in genes (ybaN and yubB) with unknown functions. Two auxotrophic mutants were identified among the 200 transposants, one with an insertion in lysA and another in a gene (yjzB) whose function is unknown.
MeSH term(s)	Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Base Sequence ; Colony Count, Microbial ; DNA Transposable Elements/genetics ; Molecular Sequence Data ; Mutagenesis, Insertional/methods ; Mutation ; Plasmids/genetics ; Sequence Analysis, DNA ; Spores, Bacterial/genetics ; Transposases/genetics ; Transposases/metabolism
Chemical Substances	DNA Transposable Elements ; Transposases (EC 2.7.7.-)
Language	English
Publishing date	2006-01
Publishing country	United States
Document type	Evaluation Studies ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	223011-2
ISSN	1098-5336 ; 0099-2240
ISSN (online)	1098-5336
ISSN	0099-2240
DOI	10.1128/AEM.72.1.327-333.2006
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