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  • 1
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    Interspecies interactions that result in Bacillus subtilis forming biofilms are mediated mainly by members of its own genus [Microbiology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-11-30
    Description: Many different systems of bacterial interactions have been described. However, relatively few studies have explored how interactions between different microorganisms might influence bacterial development. To explore such interspecies interactions, we focused on Bacillus subtilis, which characteristically develops into matrix-producing cannibals before entering sporulation. We investigated whether organisms from the natural environment of B. subtilis—the soil—were able to alter the development of B. subtilis. To test this possibility, we developed a coculture microcolony screen in which we used fluorescent reporters to identify soil bacteria able to induce matrix production in B. subtilis. Most of the bacteria that influence matrix production in B. subtilis are members of the genus Bacillus, suggesting that such interactions may be predominantly with close relatives. The interactions we observed were mediated via two different mechanisms. One resulted in increased expression of matrix genes via the activation of a sensor histidine kinase, KinD. The second was kinase independent and conceivably functions by altering the relative subpopulations of B. subtilis cell types by preferentially killing noncannibals. These two mechanisms were grouped according to the inducing strain's relatedness to B. subtilis. Our results suggest that bacteria preferentially alter their development in response to secreted molecules from closely related bacteria and do so using mechanisms that depend on the phylogenetic relatedness of the interacting bacteria.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    Biofilm induction by plant polysaccharides [Microbiology] (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-04-24
    Description: Bacillus subtilis is a plant-beneficial Gram-positive bacterium widely used as a biofertilizer. However, relatively little is known regarding the molecular processes underlying this bacterium's ability to colonize roots. In contrast, much is known about how this bacterium forms matrix-enclosed multicellular communities (biofilms) in vitro. Here, we show that, when B....
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 3
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    Microbiology. Deadly priming (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolter, Roberto -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA. rkolter@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962544" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Colony Count, Microbial ; Escherichia coli/cytology/*physiology ; Glucosephosphate Dehydrogenase/*metabolism ; Oligopeptides/*metabolism ; *Quorum Sensing ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    D-amino acids trigger biofilm disassembly (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-05-01
    Description: Bacteria form communities known as biofilms, which disassemble over time. In our studies outlined here, we found that, before biofilm disassembly, Bacillus subtilis produced a factor that prevented biofilm formation and could break down existing biofilms. The factor was shown to be a mixture of D-leucine, D-methionine, D-tyrosine, and D-tryptophan that could act at nanomolar concentrations. D-amino acid treatment caused the release of amyloid fibers that linked cells in the biofilm together. Mutants able to form biofilms in the presence of D-amino acids contained alterations in a protein (YqxM) required for the formation and anchoring of the fibers to the cell. D-amino acids also prevented biofilm formation by Staphylococcus aureus and Pseudomonas aeruginosa. D-amino acids are produced by many bacteria and, thus, may be a widespread signal for biofilm disassembly.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2921573/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2921573/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolodkin-Gal, Ilana -- Romero, Diego -- Cao, Shugeng -- Clardy, Jon -- Kolter, Roberto -- Losick, Richard -- CA24487/CA/NCI NIH HHS/ -- GM086258/GM/NIGMS NIH HHS/ -- GM18546/GM/NIGMS NIH HHS/ -- GM58213/GM/NIGMS NIH HHS/ -- R01 GM018568/GM/NIGMS NIH HHS/ -- R01 GM018568-39/GM/NIGMS NIH HHS/ -- R01 GM058213/GM/NIGMS NIH HHS/ -- R01 GM086258/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Apr 30;328(5978):627-9. doi: 10.1126/science.1188628.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20431016" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*metabolism/pharmacology ; Bacillus subtilis/*physiology ; Bacterial Proteins/chemistry/metabolism ; *Biofilms/growth & development ; Cell Wall ; Culture Media, Conditioned ; Genes, Bacterial ; Leucine/metabolism/pharmacology ; Methionine/metabolism/pharmacology ; Molecular Sequence Data ; Mutation ; Pseudomonas aeruginosa/physiology ; Staphylococcus aureus/physiology ; Stereoisomerism ; Tryptophan/metabolism/pharmacology ; Tyrosine/metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    One for all and all for one (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolter, R -- Losick, R -- New York, N.Y. -- Science. 1998 Apr 10;280(5361):226-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Harvard Medical School, Boston, MA 02115, USA. kolter@mbcrr.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9565532" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Butyrolactone/*analogs & derivatives/metabolism ; Bacterial Adhesion ; *Bacterial Physiological Phenomena ; Biofilms/*growth & development ; Homoserine/*analogs & derivatives/metabolism ; Pseudomonas aeruginosa/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Microbial competition: Escherichia coli mutants that take over stationary phase cultures (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: Many microorganisms, including Escherichia coli, can survive extended periods of starvation. The properties of cells that survived prolonged incubation in stationary phase were studied by mixture of 10-day-old (aged) cultures with 1-day-old (young) cultures of the same strain of Escherichia coli. Mutants from the aged cultures that could grow eventually took over the population, which resulted in the death of the cells from the young cultures. This phenotype was conferred by mutations in rpoS, which encodes a putative stationary phase-specific sigma factor. These rapid population shifts have implications for the studies of microbial evolution and ecology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zambrano, M M -- Siegele, D A -- Almiron, M -- Tormo, A -- Kolter, R -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1757-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681219" target="_blank"〉PubMed〈/a〉
    Keywords: Acridine Orange ; Alleles ; Amino Acid Sequence ; Cloning, Molecular ; Escherichia coli/*genetics/*growth & development/physiology ; Hydrogen Peroxide/metabolism ; Molecular Sequence Data ; *Mutation ; Peroxidase/metabolism ; Phenotype ; Sigma Factor/chemistry/*genetics ; Staining and Labeling ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Pseudomonas-Candida interactions: an ecological role for virulence factors (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-06-22
    Description: Bacterial-fungal interactions have great environmental, medical, and economic importance, yet few have been well characterized at the molecular level. Here, we describe a pathogenic interaction between Pseudomonas aeruginosa and Candida albicans, two opportunistic pathogens. P. aeruginosa forms a dense biofilm on C. albicans filaments and kills the fungus. In contrast, P. aeruginosa neither binds to nor kills yeast-form C. albicans. Several P. aeruginosa virulence factors that are important in disease are involved in the killing of C. albicans filaments. We propose that many virulence factors studied in the context of human infection may also have a role in bacterial-fungal interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogan, Deborah A -- Kolter, Roberto -- GM58213/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2229-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077418" target="_blank"〉PubMed〈/a〉
    Keywords: Antibiosis ; Bacterial Adhesion ; Bacterial Proteins/physiology ; *Biofilms ; Candida albicans/genetics/growth & development/*pathogenicity/*physiology ; Ecosystem ; Fimbriae, Bacterial/physiology ; Flagella/physiology ; Fungal Proteins/physiology ; Genes, Bacterial ; Genes, Fungal ; Mutation ; Phenotype ; Pseudomonas aeruginosa/genetics/growth & development/*pathogenicity/*physiology ; Virulence/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: Esherichia coli microcin B17 is a posttranslationally modified peptide that inhibits bacterial DNA gyrase. It contains four oxazole and four thiazole rings and is representative of a broad class of pharmaceutically important natural products with five-membered heterocycles derived from peptide precursors. An in vitro assay was developed to detect heterocycle formation, and an enzyme complex, microcin B17 synthase, was purified and found to contain three proteins, McbB, McbC, and McbD, that convert 14 residues into the eight mono- and bisheterocyclic moieties in vitro that confer antibiotic activity on mature microcin B17. These enzymatic reactions alter the peptide backbone connectivity. The propeptide region of premicrocin is the major recognition determinant for binding and downstream heterocycle formation by microcin B17 synthase. A general pathway for the enzymatic biosynthesis of these heterocycles is formulated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Y M -- Milne, J C -- Madison, L L -- Kolter, R -- Walsh, C T -- 5T32AI07410-03/AI/NIAID NIH HHS/ -- 5T32GM07306-19/GM/NIGMS NIH HHS/ -- GM20011/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1188-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895467" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Anti-Bacterial Agents/*biosynthesis/chemistry/pharmacology ; *Bacterial Proteins ; Bacteriocins/*biosynthesis/chemistry/genetics/pharmacology ; Enzyme Inhibitors/pharmacology ; Escherichia coli/*enzymology/genetics ; Molecular Weight ; Multienzyme Complexes/genetics/*isolation & purification/*metabolism ; Operon ; Oxazoles/analysis ; Oxidation-Reduction ; Oxygen/metabolism ; Protein Precursors/biosynthesis/genetics ; Protein Processing, Post-Translational ; Substrate Specificity ; Thiazoles/analysis ; Topoisomerase II Inhibitors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-24
    Description: Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. In this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babbitt, P C -- Mrachko, G T -- Hasson, M S -- Huisman, G W -- Kolter, R -- Ringe, D -- Petsko, G A -- Kenyon, G L -- Gerlt, J A -- GM-34572/GM/NIGMS NIH HHS/ -- GM-40570/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1159-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855594" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Histidine/metabolism ; Hydro-Lyases/chemistry/genetics/*metabolism ; *Intramolecular Lyases ; Isomerases/chemistry/*metabolism ; Lysine/metabolism ; Molecular Sequence Data ; Open Reading Frames ; Operon ; *Protons ; Pseudomonas putida/*enzymology/genetics ; Racemases and Epimerases/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Sensing starvation: a homoserine lactone--dependent signaling pathway in Escherichia coli (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: When nutrients become limiting, many bacteria differentiate and become resistant to environmental stresses. For Escherichia coli, this process is mediated by the sigma s subunit of RNA polymerase. Expression of sigma s was induced by homoserine lactone, a metabolite synthesized from intermediates in threonine biosynthesis. Homoserine lactone-dependent synthesis of sigma s was prevented by overexpression of a newly identified protein, RspA. The function of homoserine lactone derivatives in many cell density-dependent phenomena and the similarity of RspA to a Streptomyces ambofaciens protein suggest that synthesis of homoserine lactone may be a general signal of starvation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huisman, G W -- Kolter, R -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):537-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545940" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Butyrolactone/*analogs & derivatives/metabolism/pharmacology ; Amino Acid Sequence ; Bacterial Proteins/*biosynthesis/chemistry/genetics/metabolism ; Catalase/metabolism ; Escherichia coli/genetics/*metabolism ; Gene Expression Regulation, Bacterial ; Models, Biological ; Molecular Sequence Data ; Operon ; Phenotype ; Sigma Factor/*biosynthesis/genetics ; *Signal Transduction ; Transcription, Genetic ; Vibrio/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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