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Article ; Online: A Pilot and Feasibility Mobile Health Intervention to Support Healthy Behaviors in African American Breast Cancer Survivors.

Allicock, Marlyn / Kendzor, Darla / Sedory, Abigail / Gabriel, Kelley Pettee / Swartz, Michael D / Thomas, Priya / Yudkin, Joshua S / Rivers, Aeisha

Journal of racial and ethnic health disparities

2020 Volume 8, Issue 1, Page(s) 157–165

Abstract: African American breast cancer (AA BC) survivors are more likely to have cancer-related comorbidities compared with other women, ultimately putting them at higher risk for overall mortality and breast cancer-specific mortality. Survivorship care ... ...

Abstract	African American breast cancer (AA BC) survivors are more likely to have cancer-related comorbidities compared with other women, ultimately putting them at higher risk for overall mortality and breast cancer-specific mortality. Survivorship care guidelines emphasize the importance of attention to obesity, weight management, and physical activity. Mobile technologies have been effective for improving health behaviors among cancer survivors, though few studies have focused on AA BC survivors. Creating Healthy Actions through Technology (CHAT) was a 4-week pilot intervention that employed an ecological momentary assessment (EMA) to improve survivors' physical activity and diet behaviors. We evaluated the acceptability, feasibility, and impact of a mHealth intervention for AA BC survivors. Participants (N = 22) were randomized to intervention (n = 13) or control (n = 9). All participants completed daily EMAs via smartphone for 4 weeks and wore accelerometers for seven consecutive days at baseline, 4, and 8 weeks. Intervention participants additionally received tailored health messages. Diet was measured using a self-reported questionnaire and physical activity with accelerometers. Participant engagement was high. Of 84 EMA assessments, the average response was 63 (SD 16.1). Participant accelerometer wear was at least 6 of the 7 days (SD 1.7) for each assessment. Eighty-five percent of participants reported the intervention helped change behaviors. Intervention participants reduced their sedentary time by 4.37 (SD = 7.14) hours/day versus controls (p = .05), reduced fast food intake by 1.5 servings (p = 0.008), and increased vigorous activity by 0.56 (SD = 28.10) minutes, which was non-significant (p = 0.959). Findings show feasibility and acceptability and potential of the intervention to positively impact physical activity among AA BC survivors.
MeSH term(s)	Adult ; African Americans/psychology ; African Americans/statistics & numerical data ; Breast Neoplasms/ethnology ; Cancer Survivors/psychology ; Cancer Survivors/statistics & numerical data ; Feasibility Studies ; Female ; Health Behavior/ethnology ; Humans ; Middle Aged ; Pilot Projects ; Surveys and Questionnaires ; Telemedicine
Language	English
Publishing date	2020-05-08
Publishing country	Switzerland
Document type	Journal Article ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
ZDB-ID	2760524-3
ISSN	2196-8837 ; 2197-3792
ISSN (online)	2196-8837
ISSN	2197-3792
DOI	10.1007/s40615-020-00767-x
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Article: Differential gene expression in genetically identical sister cells: the initiation of sporulation in Bacillus subtilis.

Yudkin, Michael D / Clarkson, Joanna

Molecular microbiology

2005 Volume 56, Issue 3, Page(s) 578–589

Abstract: Early in sporulation, the cell divides asymmetrically to give two sister compartments, a smaller prespore and a larger mother cell. Differential gene expression in these compartments depends on the regulation of the first sporulation-specific sigma ... ...

Abstract	Early in sporulation, the cell divides asymmetrically to give two sister compartments, a smaller prespore and a larger mother cell. Differential gene expression in these compartments depends on the regulation of the first sporulation-specific sigma factor, sigma(F), which is activated only in the prespore. Regulation relies on the interactions of four proteins -sigma(F), its antisigma SpoIIAB (which also has protein kinase activity), the anti-antisigma SpoIIAA and the protein phosphatase SpoIIE. Before asymmetric division, and in the mother cell after division, sigma(F) is held in an inactive complex with SpoIIAB and ATP; SpoIIAA is in its phosphorylated form. To disrupt the complex so as to liberate sigma(F) in the prespore, dephosphorylated SpoIIAA is needed, and this is made available by SpoIIE. Thereafter, SpoIIAB and SpoIIE are active simultaneously in the prespore, cycling SpoIIAA through phosphorylated and non-phosphorylated forms. This cycle detains SpoIIAB in a state in which it cannot inhibit sigma(F). Results from biophysical techniques, mathematical simulations and enzyme kinetics have now helped to elucidate the dynamics of the protein-protein interactions involved. An understanding of these dynamics largely accounts for the regulation of sigma(F). We show that the system is tuned to be highly efficient in its use of components and extremely economical in conserving ATP.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Bacillus subtilis/genetics ; Bacillus subtilis/physiology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Mutation ; Phosphorylation ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Spores, Bacterial/genetics ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Bacterial Proteins ; Sigma Factor ; Transcription Factors ; spore-specific proteins, Bacillus ; sporulation-specific sigma factors ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2005-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/j.1365-2958.2005.04594.x
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Article: Physical evidence for the induced release of the Bacillus subtilis transcription factor, sigma(F), from its inhibitory complex.

Clarkson, Joanna / Campbell, Iain D / Yudkin, Michael D

Journal of molecular biology

2004 Volume 340, Issue 2, Page(s) 203–209

Abstract: The release of the transcription factor sigma(F) from its inhibitory complex with SpoIIAB is a key regulatory step in the control of sporulation in Bacillus subtilis as it initiates a pattern of differential gene expression in the mother cell and ... ...

Abstract	The release of the transcription factor sigma(F) from its inhibitory complex with SpoIIAB is a key regulatory step in the control of sporulation in Bacillus subtilis as it initiates a pattern of differential gene expression in the mother cell and prespore compartments. The sigma(F).SpoIIAB complex is dissociated by the unphosphorylated form of the protein SpoIIAA, the alternative binding partner of SpoIIAB. Here, we employ fluorescence spectroscopy to examine the mechanism by which SpoIIAA acts on the sigma(F).SpoIIAB complex. We constructed a mutant of sigma(F), sigma(F)-W46L, which displayed a reproducible fluorescence response on binding to SpoIIAB. Using this mutant we were able to quantify the amount of sigma(F) bound to SpoIIAB in real time. The results provide physical evidence for the "induced release" mechanism of sigma(F) activation. We demonstrate that SpoIIAA interacts directly with the sigma(F).SpoIIAB complex, greatly decreasing the affinity of SpoIIAB for sigma(F) and thus causing the release of the latter. We also demonstrate that sigma(F) is released before SpoIIAA is phosphorylated and that release occurs on a similar time scale to the binding of SpoIIAA to SpoIIAB.
MeSH term(s)	Bacillus subtilis/metabolism ; Bacterial Proteins/metabolism ; Base Sequence ; DNA Primers ; Kinetics ; Reproducibility of Results ; Sigma Factor/metabolism ; Spectrometry, Fluorescence
Chemical Substances	Bacterial Proteins ; DNA Primers ; FliA protein, Bacteria ; Sigma Factor ; spore-specific proteins, Bacillus
Language	English
Publishing date	2004-07-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2004.04.061
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Article: Efficient regulation of sigmaF, the first sporulation-specific sigma factor in B.subtilis.

Clarkson, Joanna / Campbell, Iain D / Yudkin, Michael D

Journal of molecular biology

2004 Volume 342, Issue 4, Page(s) 1187–1195

Abstract: Differential gene expression is established in the prespore and mother-cell compartments of Bacillus subtilis through the successive activation of a series of cell-type-specific sigma factors. Crucial to the success of this process is the control of the ... ...

Abstract	Differential gene expression is established in the prespore and mother-cell compartments of Bacillus subtilis through the successive activation of a series of cell-type-specific sigma factors. Crucial to the success of this process is the control of the first prespore-specific sigma factor, sigmaF. sigmaF is regulated by the proteins SpoIIAB, SpoIIAA and SpoIIE. SpoIIAB forms an inhibitory complex with sigmaF, which can be dissociated by interaction with SpoIIAA. During this interaction SpoIIAA is phosphorylated. SpoIIE is a membrane-bound phosphatase that dephosphorylates SpoIIAA, thereby re-activating it. It is not understood how sigmaF is activated specifically in the prespore but not in the mother cell. Here, we use a recently developed fluorescence spectroscopy technique to follow in real time the formation of sigmaF.SpoIIAB complexes and their dissociation by SpoIIAA. We show that complete activation of sigmaF is induced by a tenfold increase in SpoIIE activity. This result demonstrates that relatively small changes in SpoIIE activity, which could arise from asymmetric septation, can achieve the all-or-nothing response in sigmaF activity required by the cell. For long-term sigmaF activation, we find that sustained SpoIIE activity is required to counteract the activity of SpoIIAB. Even though the continual phosphorylation and dephosphorylation of SpoIIAA by these two enzymes will expend some ATP, the formation of SpoIIAA.SpoIIAB.ADP complexes greatly diminishes the rate of the phosphorylation reaction, and thus minimizes the wastage of energy. These features provide a very efficient system for regulating sigmaF.
MeSH term(s)	Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Bacillus subtilis/genetics ; Bacillus subtilis/physiology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Phosphorylation ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Spectrometry, Fluorescence ; Spores, Bacterial
Chemical Substances	Bacterial Proteins ; FliA protein, Bacteria ; Sigma Factor ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2004-09-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2004.07.090
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Article ; Online: The mechanism of cell differentiation in Bacillus subtilis.

Iber, Dagmar / Clarkson, Joanna / Yudkin, Michael D / Campbell, Iain D

Nature

2006 Volume 441, Issue 7091, Page(s) 371–374

Abstract: Sporulation in Bacillus subtilis serves as a model for the development of two different cell types from a single cell. Although much information has been accumulated about the mechanisms that initiate the developmental programmes, important questions ... ...

Abstract	Sporulation in Bacillus subtilis serves as a model for the development of two different cell types from a single cell. Although much information has been accumulated about the mechanisms that initiate the developmental programmes, important questions remain that can be answered only by quantitative analysis. Here we develop, with the help of existing and new experimental results, a mathematical model that reproduces published in vitro experiments and explains how the activation of the key transcription factor is regulated. The model identifies the difference in volume between the two cell types as the primary trigger for determining cell fate. It shows that this effect depends on the allosteric behaviour of a key protein kinase and on a low rate of dephosphorylation by the corresponding phosphatase; both predicted effects are confirmed experimentally.
MeSH term(s)	Allosteric Regulation ; Bacillus subtilis/cytology ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/metabolism ; Cell Differentiation ; Cell Lineage ; DNA-Directed RNA Polymerases/metabolism ; Gene Expression Regulation, Bacterial ; Holoenzymes/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Sigma Factor/metabolism ; Spores, Bacterial/cytology ; Spores, Bacterial/metabolism
Chemical Substances	Bacterial Proteins ; FliA protein, Bacteria ; Holoenzymes ; Sigma Factor ; spore-specific proteins, Bacillus ; Protein Kinases (EC 2.7.-) ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
Language	English
Publishing date	2006-05-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature04666
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Article: Phosphorylation induces subtle structural changes in SpoIIAA, a key regulator of sporulation.

Clarkson, Joanna / Campbell, Iain D / Yudkin, Michael D

The Biochemical journal

2003 Volume 372, Issue Pt 1, Page(s) 113–119

Abstract: The phosphorylation state of SpoIIAA is a key factor in the regulation of sporulation in Bacillus subtilis. Previous crystallographic studies had led to the conclusion that phosphorylation alters the binding affinity of SpoIIAA for its partner proteins ... ...

Abstract	The phosphorylation state of SpoIIAA is a key factor in the regulation of sporulation in Bacillus subtilis. Previous crystallographic studies had led to the conclusion that phosphorylation alters the binding affinity of SpoIIAA for its partner proteins solely through the additional charge and bulk of the phosphoryl group: small structural changes observed elsewhere in the protein were considered to be random fluctuations rather than the result of phosphorylation. The results presented in the present paper show that NMR studies detect the same subtle structural changes in solution as those seen in the crystal, strongly implying that they are the direct result of phosphorylation. These subtle structural changes are similar to those that occur in a non-phosphorylated mutant that is defective in binding to one of its partner proteins. We propose that the structural changes which occur in SpoIIAA on phosphorylation act in concert with the phosphoryl group to alter its binding properties.
MeSH term(s)	Bacillus subtilis/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Crystallography, X-Ray ; Histidine/metabolism ; Kinetics ; Magnetic Resonance Spectroscopy ; Mutation ; Phosphorylation ; Protein Conformation ; Protein Structure, Tertiary
Chemical Substances	Bacterial Proteins ; spore-specific proteins, Bacillus ; Histidine (4QD397987E)
Language	English
Publishing date	2003-05-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
ISSN (online)	1470-8728
ISSN	0264-6021 ; 0006-2936 ; 0306-3275
DOI	10.1042/BJ20021748
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Article: Phosphorylation and RsbX-dependent dephosphorylation of RsbR in the RsbR-RsbS complex of Bacillus subtilis.

Chen, Chien-Cheng / Yudkin, Michael D / Delumeau, Olivier

Journal of bacteriology

2004 Volume 186, Issue 20, Page(s) 6830–6836

Abstract: In the pathway that controls sigmaB activity, the RsbR-RsbS complex plays an important role by trapping RsbT, a positive regulator of sigmaB of Bacillus subtilis. We have proposed that at the onset of stress, RsbR becomes phosphorylated, resulting in an ... ...

Abstract	In the pathway that controls sigmaB activity, the RsbR-RsbS complex plays an important role by trapping RsbT, a positive regulator of sigmaB of Bacillus subtilis. We have proposed that at the onset of stress, RsbR becomes phosphorylated, resulting in an enhanced activity of RsbT towards RsbS. RsbT is then free to interact with and activate RsbU, which in turn ultimately activates sigmaB. In this study with purified proteins, we used mutant RsbR proteins to analyze the role of its phosphorylatable threonine residues. The results show that the phosphorylation of either of the two RsbT-phosphorylatable threonine residues (T171 and T205) in RsbR enhanced the kinase activity of RsbT towards RsbS. However, it appeared that RsbT preferentially phosphorylates T171. We also present in vitro evidence that identifies RsbX as a potential phosphatase for RsbR T205.
MeSH term(s)	Bacillus subtilis/enzymology ; Bacillus subtilis/genetics ; Bacillus subtilis/physiology ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Mutagenesis, Site-Directed ; Mutation ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Sigma Factor/metabolism ; Signal Transduction
Chemical Substances	Bacterial Proteins ; Phosphoproteins ; RsbR protein, Bacillus subtilis ; SigB protein, Bacteria ; Sigma Factor ; RsbT protein, Bacillus subtilis (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
Language	English
Publishing date	2004-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.186.20.6830-6836.2004
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Article ; Online: Studies of SpoIIAB mutant proteins elucidate the mechanisms that regulate the developmental transcription factor sigmaF in Bacillus subtilis.

Shu, Jwu-Ching / Clarkson, Joanna / Yudkin, Michael D

The Biochemical journal

2004 Volume 384, Issue Pt 1, Page(s) 169–178

Abstract: SigmaF, the first compartment-specific sigma factor of sporulation, is regulated by an anti-sigma factor, SpoIIAB (AB) and its antagonist SpoIIAA (AA). AB can bind to sigmaF in the presence of ATP or to AA in the presence of ADP; in addition, AB can ... ...

Abstract	SigmaF, the first compartment-specific sigma factor of sporulation, is regulated by an anti-sigma factor, SpoIIAB (AB) and its antagonist SpoIIAA (AA). AB can bind to sigmaF in the presence of ATP or to AA in the presence of ADP; in addition, AB can phosphorylate AA. The ability of AB to switch between its two binding partners regulates sigmaF. Early in sporulation, AA activates sigmaF by releasing it from its complex with AB. We have previously proposed a reaction scheme for the phosphorylation of AA by AB which accounts for AA's regulatory role. A crucial feature of this scheme is a conformational change in AB that accompanies its switch in binding partner. In the present study, we have studied three AB mutants, all of which have amino-acid replacements in the nucleotide-binding region; AB-E104K (Glu104-->Lys) and AB-T49K (Thr49-->Lys) fail to activate sigmaF, and AB-R105A (Arg105-->Ala) activates it prematurely. We used techniques of enzymology, surface plasmon resonance and fluorescence spectroscopy to analyse the defects in each mutant. AB-E104K was deficient in binding to AA, AB-T49K was deficient in binding to ADP and AB-R105A bound ADP exceptionally strongly. Although the release of sigmaF from all three mutant proteins was impaired, and all three failed to undergo the wild-type conformational change when switching binding partners, the phenotypes of the mutant cells were best accounted for by the properties of the respective AB species in forming complexes with AA and ADP. The behaviour of the mutants enables us to propose convincing mechanisms for the regulation of sigmaF in wild-type bacteria.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Alanine/genetics ; Alanine/physiology ; Amino Acid Substitution/physiology ; Arginine/genetics ; Arginine/physiology ; Bacillus subtilis/genetics ; Bacterial Proteins/antagonists & inhibitors ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Proteins/physiology ; Glutamic Acid ; Kinetics ; Lysine/genetics ; Lysine/physiology ; Multiprotein Complexes/metabolism ; Mutation/genetics ; Mutation/physiology ; Nucleotides/metabolism ; Phenotype ; Phosphorylation ; Sigma Factor/metabolism ; Sigma Factor/physiology ; Threonine/genetics ; Threonine/physiology
Chemical Substances	Bacterial Proteins ; Multiprotein Complexes ; Nucleotides ; Sigma Factor ; spore-specific proteins, Bacillus ; Threonine (2ZD004190S) ; Glutamic Acid (3KX376GY7L) ; Adenosine Triphosphate (8L70Q75FXE) ; Arginine (94ZLA3W45F) ; Lysine (K3Z4F929H6) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2004-11-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20040923
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Article: Protein-protein interactions that regulate the energy stress activation of sigma(B) in Bacillus subtilis.

Delumeau, Olivier / Lewis, Richard J / Yudkin, Michael D

Journal of bacteriology

2001 Volume 184, Issue 20, Page(s) 5583–5589

Abstract: Sigma(B) is an alternative sigma factor that controls the general stress response in Bacillus subtilis. In the absence of stress, sigma(B) is negatively regulated by anti-sigma factor RsbW. RsbW is also a protein kinase which can phosphorylate RsbV. When ...

Abstract	Sigma(B) is an alternative sigma factor that controls the general stress response in Bacillus subtilis. In the absence of stress, sigma(B) is negatively regulated by anti-sigma factor RsbW. RsbW is also a protein kinase which can phosphorylate RsbV. When cells are stressed, RsbW binds to unphosphorylated RsbV, produced from the phosphorylated form of RsbV by two phosphatases (RsbU and RsbP) which are activated by stress. We now report the values of the K(m) for ATP and the K(i) for ADP of RsbW (0.9 and 0.19 mM, respectively), which reinforce the idea that the kinase activity of RsbW is directly regulated in vivo by the ratio of these nucleotides. RsbW, purified as a dimer, forms complexes with RsbV and sigma(B) with different stoichiometries, i.e., RsbW(2)-RsbV(2) and RsbW(2)-sigma(B)(1). As determined by surface plasmon resonance, the dissociation constants of the RsbW-RsbV and RsbW-sigma(B) interactions were found to be similar (63 and 92 nM, respectively). Nonetheless, an analysis of the complexes by nondenaturing polyacrylamide gel electrophoresis in competition assays suggested that the affinity of RsbW(2) for RsbV is much higher than that for sigma(B). The intracellular concentrations of RsbV, RsbW (as a monomer), and sigma(B) measured before stress were similar (1.5, 2.6, and 0.9 micro M, respectively). After ethanol stress they all increased. The increase was greatest for RsbV, whose concentration reached 13 micro M, while those of RsbW (as a monomer) and sigma(B) reached 11.8 and 4.9 micro M, respectively. We conclude that the higher affinity of RsbW for RsbV than for sigma(B), rather than a difference in the concentrations of RsbV and sigma(B), is the driving force that is responsible for the switch of RsbW to unphosphorylated RsbV.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacillus subtilis/physiology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding, Competitive ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Heat-Shock Response ; Kinetics ; Phosphoric Monoester Hydrolases ; Protein Binding ; Sigma Factor/genetics ; Sigma Factor/metabolism
Chemical Substances	Bacterial Proteins ; Carrier Proteins ; RsbV protein, Bacteria ; RsbW protein, bacteria ; SigB protein, Bacteria ; Sigma Factor ; Adenosine Triphosphate (8L70Q75FXE) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; RsbU protein, Bacillus subtilis (EC 3.1.3.3)
Language	English
Publishing date	2001-10-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.184.20.5583-5589.2002
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Article: Evaluation of the kinetic properties of the sporulation protein SpoIIE of Bacillus subtilis by inclusion in a model membrane.

Searls, Tim / Chen, Xingyong / Allen, Stephanie / Yudkin, Michael D

Journal of bacteriology

2004 Volume 186, Issue 10, Page(s) 3195–3201

Abstract: Starvation induces Bacillus subtilis to initiate a developmental process (sporulation) that includes asymmetric cell division to form the prespore and the mother cell. The integral membrane protein SpoIIE is essential for the prespore-specific activation ...

Abstract	Starvation induces Bacillus subtilis to initiate a developmental process (sporulation) that includes asymmetric cell division to form the prespore and the mother cell. The integral membrane protein SpoIIE is essential for the prespore-specific activation of the transcription factor sigmaF, and it also has a morphogenic activity required for asymmetric division. An increase in the local concentration of SpoIIE at the polar septum of B. subtilis precedes dephosphorylation of the anti-anti-sigma factor SpoIIAA in the prespore. After closure and invagination of the asymmetric septum, phosphatase activity of SpoIIE increases severalfold, but the reason for this dramatic change in activity has not been determined. The central domain of SpoIIE has been seen to self-associate (I. Lucet et al., EMBO J. 19:1467-1475, 2000), suggesting that activation of the C-terminal PP2C-like phosphatase domain might be due to conformational changes brought about by the increased local concentration of SpoIIE in the sporulating septum. Here we report the inclusion of purified SpoIIE protein into a model membrane as a method for studying the effect of local concentration in a lipid bilayer on activity. In vitro assays indicate that the membrane-bound enzyme maintains dephosphorylation rates similar to the highly active micellar state at all molar ratios of protein to lipid. Atomic force microscopy images indicate that increased local concentration does not lead to self-association.
MeSH term(s)	Bacillus subtilis/chemistry ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Kinetics ; Lipid Bilayers/chemistry ; Microscopy, Atomic Force
Chemical Substances	Bacterial Proteins ; Lipid Bilayers ; spore-specific proteins, Bacillus
Language	English
Publishing date	2004-02-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.186.10.3195-3201.2004
Database	MEDical Literature Analysis and Retrieval System OnLINE

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