The Bacillus subtilis dCMP deaminase ComEB acts as a dynamic polar localization factor for ComGA within the competence machinery

2020 ◽  
Vol 113 (5) ◽  
pp. 906-922 ◽  
Author(s):  
Marie Burghard‐Schrod ◽  
Stephan Altenburger ◽  
Peter L. Graumann
Keyword(s):  
Bacillus Subtilis ◽  
Polar Localization ◽  
Localization Factor

scholarly journals Dissection of functional domains of the polar localization factor PodJ in Caulobacter crescentus

2006 ◽  
Vol 59 (1) ◽  
pp. 301-316 ◽  
Author(s):  
Melanie L. Lawler ◽  
David E. Larson ◽  
Aaron J. Hinz ◽  
David Klein ◽  
Yves V. Brun
Keyword(s):  
Caulobacter Crescentus ◽  
Functional Domains ◽  
Polar Localization ◽  
Localization Factor

scholarly journals DivIVA-Mediated Polar Localization of ComN, a Posttranscriptional Regulator of Bacillus subtilis

2012 ◽  
Vol 194 (14) ◽  
pp. 3661-3669 ◽  
Author(s):  
V. T. dos Santos ◽  
A. W. Bisson-Filho ◽  
F. J. Gueiros-Filho
Keyword(s):  
Bacillus Subtilis ◽  
Polar Localization

scholarly journals CheR- and CheB-Dependent Chemosensory Adaptation System of Rhodobacter sphaeroides

2001 ◽  
Vol 183 (24) ◽  
pp. 7135-7144 ◽  
Author(s):  
Angela C. Martin ◽  
George H. Wadhams ◽  
Deepan S. H. Shah ◽  
Steven L. Porter ◽  
Jeevani C. Mantotta ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Rhodobacter Sphaeroides ◽  
High Abundance ◽  
E Coli ◽  
Polar Localization ◽  
Receptor Adaptation ◽  
Cell Assays ◽  
Chemotaxis Proteins ◽  
Conserved Region

ABSTRACT Rhodobacter sphaeroides has multiple homologues of most of the Escherichia coli chemotaxis genes, organized in three major operons and other, unlinked, loci. These includecheA 1 andcheR 1 (cheOp1) and cheA 2 ,cheR2 , andcheB1 (che Op2). In-frame deletions of thesecheR and cheB homologues were constructed and the chemosensory behaviour of the resultant mutants examined on swarm plates and in tethered cell assays. Under the conditions tested, CheR2 and CheB1 were essential for normal chemotaxis, whereas CheR1 was not.cheR 2 andcheB 1 , but notcheR 1 , were also able to complement the equivalent E. coli mutants. However, none of the proteins were required for the correct polar localization of the chemoreceptor McpG in R. sphaeroides. In E. coli, CheR binds to the NWETF motif on the high-abundance receptors, allowing methylation of both high- and low-abundance receptors. This motif is not contained on any R. sphaeroides chemoreceptors thus far identified, although 2 of the 13 putative chemoreceptors, McpA and TlpT, do have similar sequences. This suggests that CheR2 either interacts with the NWETF motif of E. coli methyl-accepting chemotaxis proteins (MCPs), even though its native motif may be slightly different, or with another conserved region of the MCPs. Methanol release measurements show that R. sphaeroides has an adaptation system that is different from that of Bacillus subtilis and E. coli, with methanol release measurable on the addition of attractant but not on its removal. Intriguingly, CheA2, but not CheA1, is able to phosphorylate CheB1, suggesting that signaling through CheA1 cannot initiate feedback receptor adaptation via CheB1-P.

scholarly journals Polar Localization and Compartmentalization of ClpP Proteases during Growth and Sporulation in Bacillus subtilis

2008 ◽  
Vol 190 (20) ◽  
pp. 6749-6757 ◽  
Author(s):  
James Kain ◽  
Gina G. He ◽  
Richard Losick
Keyword(s):  
Bacillus Subtilis ◽  
Mother Cell ◽  
Regulatory Networks ◽  
Fluorescent Protein ◽  
The Other ◽  
Spatial Control ◽  
Polar Localization ◽  
Cell Compartments ◽  
Green Fluorescent ◽  
Necessary And Sufficient

ABSTRACT Spatial control of proteolysis is emerging as a common feature of regulatory networks in bacteria. In the spore-forming bacterium Bacillus subtilis, the peptidase ClpP can associate with any of three ATPases: ClpC, ClpE, and ClpX. Here, we report that ClpCP, ClpEP, and ClpXP localize in foci often near the poles of growing cells and that ClpP and the ATPase are each capable of polar localization independently of the other component. A region of ClpC containing an AAA domain was necessary and sufficient for polar localization. We also report that ClpCP and ClpXP proteases differentially localize to the forespore and mother cell compartments of the sporangium during spore formation. Moreover, model substrates for each protease created by appending recognition sequences for ClpCP or ClpXP to the green fluorescent protein were preferentially eliminated from the forespore or the mother cell, respectively. Biased accumulation of ClpCP in the forespore may contribute to the cell-specific activation of the transcription factor σF by preferential ClpCP-dependent degradation of the anti-σF factor SpoIIAB.

scholarly journals Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site

1998 ◽  
Vol 12 (21) ◽  
pp. 3419-3430 ◽  
Author(s):  
A. L. Marston ◽  
H. B. Thomaides ◽  
D. H. Edwards ◽  
M. E. Sharpe ◽  
J. Errington
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Polar Localization ◽  
Division Site ◽  
The Mind ◽  
Selection Of

Use of Antibody to aid Visualization of Protein at the Termini of Bacteriophage Ø29 DNA

1980 ◽  
Vol 38 ◽  
pp. 540-541
Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly
Keyword(s):  
Electron Microscopy ◽  
Bacillus Subtilis ◽  
Dna Synthesis ◽  
Restriction Endonuclease ◽  
Protein Complex ◽  
Protein Product ◽  
Viral Dna ◽  
Small Proteins ◽  
Antibody Labeling ◽  
Subtilis Bacteriophage

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.

Antibacterial activity of Celastrol against Bacillus subtilis

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
N Padilla-Montaño ◽  
IL Bazzocchi ◽  
L Moujir
Keyword(s):  
Antibacterial Activity ◽  
Bacillus Subtilis

Mikrobizide und viruzide Aufbereitung von Dialysegeräten

2018 ◽  
Vol 22 (02) ◽  
pp. 82-89
Author(s):  
Friedrich von Rheinbaben ◽  
Oliver Riebe ◽  
Johanna Köhnlein ◽  
Sebastian Werner
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bacillus Subtilis ◽  
Phase 3 ◽  
Aspergillus Brasiliensis

ZusammenfassungZentrales Bauteil des Genius® 90 Therapie Systems ist der sogenannte Genius-Tank, dem die frische Dialyseflüssigkeit entnommen und in den die verbrauchte Lösung nach der Dialyse zurückgeführt wird. Daher kommt der sicheren Aufbereitung des Systems eine besondere Bedeutung zu. Hierfür wird ein Aufbereitungsverfahren unter Verwendung von UV-Licht in Kombination mit einem chemischen Desinfektionsmittel angewendet. Ziel der hier beschriebenen Untersuchung war es, die Wirkungsbreite und Wirkungstiefe dieses Aufbereitungsverfahrens unter praxisnahen Phase-3-Bedingungen zu ermitteln. Dazu wurde das Gerät mit Mikroorganismen und Viren künstlich kontaminiert und die Wirkung der einzelnen Verfahrensschritte ermittelt. Im Gegensatz zu der üblichen Vorgehensweise praxisnaher Untersuchungen machen Aufbereitungsverfahren medizinischer Geräte unter Phase-3-Kriterien meist eine neuartige Arbeitsweise erforderlich – im Falle der hier vorgestellten Untersuchung sogar die Konstruktion eines speziellen Geräts zur Platzierung von Keimträgen im Genius-Tank. Im Ergebnis konnte gezeigt werden, dass bereits UV-Licht allein sowie in Kombination mit einem chemischen Desinfektionsmittel unter praxisnahen Bedingungen eine sichere Wirksamkeit gegen Bakterien (Pseudomonas aeruginosa) und bakterielle Sporen (Bacillus subtilis), Schimmelpilze (Aspergillus brasiliensis) und Viren (Murines Parvovirus) besitzt.

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