ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Chromosomal rearrangement generating a composite gene for a developmental transcription factor (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-27
    Description: Differential gene expression in the mother cell chamber of sporulating cells of Bacillus subtilis is determined in part by an RNA polymerase sigma factor called sigma K (or sigma 27). The sigma K factor was assigned as the product of the sporulation gene spoIVCB on the basis of the partial aminoterminal amino acid sequence of the purified protein. The spoIVCB gene is now shown to be a truncated gene capable of specifying only the amino terminal half of sigma K. The carboxyl terminal half is specified by another sporulation gene, spoIIIC, to which spoIVCB becomes joined inframe at an intermediate stage of sporulation by site-specific recombination within a 5-base pair repeated sequence. Juxtaposition of spoIVCB and spoIIIC need not be reversible in that the mother cell and its chromosome are discarded at the end of the developmental cycle. The rearrangement of chromosomal DNA could account for the presence of sigma K selectively in the mother cell and may be a precedent for the generation of cell type-specific regulatory proteins in other developmental systems where cells undergo terminal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stragier, P -- Kunkel, B -- Kroos, L -- Losick, R -- New York, N.Y. -- Science. 1989 Jan 27;243(4890):507-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2536191" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus subtilis/*genetics/physiology ; Base Sequence ; Cloning, Molecular ; DNA Probes ; DNA Restriction Enzymes ; DNA, Bacterial/genetics ; DNA-Directed RNA Polymerases/metabolism ; *Gene Expression Regulation ; *Gene Rearrangement ; *Genes, Bacterial ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Nucleic Acid Hybridization ; Sigma Factor/genetics ; Spores, Bacterial ; Transcription Factors/*genetics
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    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
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Cannibalism by sporulating bacteria (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-21
    Description: Spore formation by the bacterium Bacillus subtilis is an elaborate developmental process that is triggered by nutrient limitation. Here we report that cells that have entered the pathway to sporulate produce and export a killing factor and a signaling protein that act cooperatively to block sister cells from sporulating and to cause them to lyse. The sporulating cells feed on the nutrients thereby released, which allows them to keep growing rather than to complete morphogenesis. We propose that sporulation is a stress-response pathway of last resort and that B. subtilis delays a commitment to spore formation by cannibalizing its siblings.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gonzalez-Pastor, Jose E -- Hobbs, Errett C -- Losick, Richard -- GM18568/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):510-3. Epub 2003 Jun 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, The Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12817086" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Bacillus subtilis/genetics/metabolism/*physiology ; Bacterial Proteins/genetics/*metabolism ; Bacteriolysis ; Gene Expression Profiling ; *Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Mutation ; Oligonucleotide Array Sequence Analysis ; *Operon ; Sigma Factor/genetics/metabolism ; Signal Transduction ; Spores, Bacterial/*physiology ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Checkpoints that couple gene expression to morphogenesis (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Losick, R -- Shapiro, L -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1227-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Laboratories, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235653" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/genetics/growth & development/*ultrastructure ; Bacterial Proteins/genetics/*metabolism ; Flagella/metabolism/*ultrastructure ; *Gene Expression Regulation, Bacterial ; Genes, Bacterial ; *Morphogenesis ; Mutation ; Sigma Factor/genetics/*metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Localization of protein implicated in establishment of cell type to sites of asymmetric division (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-27
    Description: Asymmetric division in Bacillus subtilis generates progeny cells with dissimilar fates. SpoIIE, a membrane protein required for the establishment of cell type, was shown to localize near sites of potential polar division. SpoIIE initially localizes in a bipolar pattern, coalescing at marks in the cell envelope at which asymmetric division can take place. Then, during division, SpoIIE becomes restricted to the polar septum and is lost from the distal pole. Thus, when division is complete, SpoIIE sits at the boundary between the progeny from which it dictates cell fate by the activation of a cell-specific transcription factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arigoni, F -- Pogliano, K -- Webb, C D -- Stragier, P -- Losick, R -- GM18568/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):637-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Physico-Chimique, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570022" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/*chemistry/cytology/genetics/*physiology ; Bacterial Proteins/*analysis/physiology ; *Cell Division ; Cell Membrane/chemistry ; Gene Expression ; Microscopy, Fluorescence ; Mutation ; Recombinant Fusion Proteins/analysis ; Sigma Factor/physiology ; Spores, Bacterial/*chemistry ; *Transcription Factors
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    facet.materialart.
    Unknown
    Geometric cue for protein localization in a bacterium (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-07
    Description: Proteins in bacteria often deploy to particular places within the cell, but the cues for localization are frequently mysterious. We found that the peripheral membrane protein SpoVM (VM) recognizes a geometric cue when localizing to a particular membrane during sporulation in Bacillus subtilis. Sporulation involves an inner cell maturing into a spore and an outer cell nurturing the developing spore. VM is produced in the outer cell, where it embeds in the membrane that surrounds the inner cell but not in the cytoplasmic membrane of the outer cell. We found that VM localized by discriminating between the positive curvature of the membrane surrounding the inner cell and the negative curvature of the cytoplasmic membrane. Membrane curvature could be a general cue for protein localization in bacteria.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652684/" 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/PMC2652684/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramamurthi, Kumaran S -- Lecuyer, Sigolene -- Stone, Howard A -- Losick, Richard -- GM18568/GM/NIGMS NIH HHS/ -- R01 GM018568/GM/NIGMS NIH HHS/ -- R01 GM018568-36/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Mar 6;323(5919):1354-7. doi: 10.1126/science.1169218.〈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/19265022" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Bacillus subtilis/genetics/*metabolism ; Bacterial Proteins/chemistry/*metabolism ; Cell Membrane/*metabolism/*ultrastructure ; Lipid Bilayers/metabolism ; Liposomes/metabolism ; Mutation ; Recombinant Fusion Proteins/metabolism ; Spores, Bacterial/*metabolism/physiology/ultrastructure
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...