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  1. Article ; Online: A Conversation with Susumu Tonegawa.

    Tonegawa, Susumu / Carniol, Karen

    Cold Spring Harbor symposia on quantitative biology

    2014  Volume 79, Page(s) 295–296

    MeSH term(s) Amygdala/physiology ; Animals ; Hippocampus/physiology ; Humans ; Memory/physiology ; Mice
    Language English
    Publishing date 2014
    Publishing country United States
    Document type Interview
    ISSN 1943-4456 ; 0091-7451
    ISSN (online) 1943-4456
    ISSN 0091-7451
    DOI 10.1101/sqb.2014.79.18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: A Conversation with Richard Axel.

    Axel, Richard / Carniol, Karen

    Cold Spring Harbor symposia on quantitative biology

    2014  Volume 79, Page(s) 258–259

    MeSH term(s) Animals ; Cognition ; Humans ; Odorants ; Olfactory Bulb/physiology ; Smell/physiology
    Language English
    Publishing date 2014
    Publishing country United States
    Document type Interview
    ISSN 1943-4456 ; 0091-7451
    ISSN (online) 1943-4456
    ISSN 0091-7451
    DOI 10.1101/sqb.2014.79.03
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A Conversation with Karel Svoboda.

    Svoboda, Karel / Carniol, Karen

    Cold Spring Harbor symposia on quantitative biology

    2014  Volume 79, Page(s) 293–294

    MeSH term(s) Animals ; Decision Making ; Electrophysiology ; Mice ; Neural Pathways/physiology ; Perception
    Language English
    Publishing date 2014
    Publishing country United States
    Document type Interview
    ISSN 1943-4456 ; 0091-7451
    ISSN (online) 1943-4456
    ISSN 0091-7451
    DOI 10.1101/sqb.2014.79.17
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: A Conversation with Ann Graybiel.

    Graybiel, Ann / Carniol, Karen

    Cold Spring Harbor symposia on quantitative biology

    2014  Volume 79, Page(s) 277–278

    MeSH term(s) Animals ; Behavior ; Decision Making ; Humans ; Judgment ; Macaca
    Language English
    Publishing date 2014
    Publishing country United States
    Document type Interview
    ISSN 1943-4456 ; 0091-7451
    ISSN (online) 1943-4456
    ISSN 0091-7451
    DOI 10.1101/sqb.2014.79.11
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Signal transduction, quorum-sensing, and extracellular protease activity in Enterococcus faecalis biofilm formation.

    Carniol, Karen / Gilmore, Michael S

    Journal of bacteriology

    2004  Volume 186, Issue 24, Page(s) 8161–8163

    MeSH term(s) Biofilms/growth & development ; Enterococcus faecalis/enzymology ; Enterococcus faecalis/growth & development ; Gelatinases/genetics ; Gelatinases/metabolism ; Gene Expression Regulation, Bacterial ; Humans ; Metalloendopeptidases/genetics ; Metalloendopeptidases/metabolism ; Signal Transduction
    Chemical Substances Gelatinases (EC 3.4.24.-) ; Metalloendopeptidases (EC 3.4.24.-)
    Language English
    Publishing date 2004-12
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.186.24.8161-8163.2004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: A threshold mechanism governing activation of the developmental regulatory protein sigma F in Bacillus subtilis.

    Carniol, Karen / Eichenberger, Patrick / Losick, Richard

    The Journal of biological chemistry

    2004  Volume 279, Issue 15, Page(s) 14860–14870

    Abstract: The RNA polymerase sigma factor sigma(F) is a developmental regulatory protein that is activated in a cell-specific manner following the formation of the polar septum during the process of spore formation in the bacterium Bacillus subtilis. Activation of ...

    Abstract The RNA polymerase sigma factor sigma(F) is a developmental regulatory protein that is activated in a cell-specific manner following the formation of the polar septum during the process of spore formation in the bacterium Bacillus subtilis. Activation of sigma(F) depends on the membrane-bound phosphatase SpoIIE, which localizes to the septum, and on the formation of the polar septum itself. SpoIIE is responsible for dephosphorylating and thereby activating the phosphoprotein SpoIIAA, which, in turn, triggers the release of sigma(F) from the anti-sigma(F) factor SpoIIAB. Paradoxically, however, the presence of unphosphorylated SpoIIAA is insufficient to cause sigma(F) activation as SpoIIAA reaches substantial levels in mutants blocked in polar septation. We now describe mutants of SpoIIE, SpoIIAA, and SpoIIAB that break the dependence of sigma(F) activation on polar division. Analysis of these mutants indicates that unphosphorylated SpoIIAA must reach a threshold concentration in order to trigger the release of sigma(F) from SpoIIAB. Evidence is presented that this threshold is created by the action of SpoIIAB, which can form an alternative, long lived complex with SpoIIAA. We propose that formation of the SpoIIAA-SpoIIAB complex serves as a sink that traps SpoIIAA in an inactive state and that only when unphosphorylated SpoIIAA is in excess to the sink does activation of sigma(F) take place.
    MeSH term(s) Amino Acid Sequence ; Bacillus subtilis/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Cell Membrane/metabolism ; Immunoblotting ; Isoelectric Focusing ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Plasmids/metabolism ; Protein Binding ; Sequence Homology, Amino Acid ; Sigma Factor/chemistry ; Sigma Factor/metabolism ; Time Factors ; beta-Galactosidase/metabolism
    Chemical Substances Bacterial Proteins ; FliA protein, Bacteria ; Sigma Factor ; spore-specific proteins, Bacillus ; beta-Galactosidase (EC 3.2.1.23)
    Language English
    Publishing date 2004-01-26
    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 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M314274200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Evidence in support of a docking model for the release of the transcription factor sigma F from the antisigma factor SpoIIAB in Bacillus subtilis.

    Ho, Margaret S / Carniol, Karen / Losick, Richard

    The Journal of biological chemistry

    2003  Volume 278, Issue 23, Page(s) 20898–20905

    Abstract: Cell-specific activation of the transcription factor sigmaF during the process of sporulation in Bacillus subtilis is governed by an antisigma factor SpoIIAB and an anti-antisigma factor SpoIIAA. SpoIIAB, which exists as a dimer, binds to sigmaF in a ... ...

    Abstract Cell-specific activation of the transcription factor sigmaF during the process of sporulation in Bacillus subtilis is governed by an antisigma factor SpoIIAB and an anti-antisigma factor SpoIIAA. SpoIIAB, which exists as a dimer, binds to sigmaF in a complex of stoichiometry sigmaF.SpoIIAB2. Escape from the complex is mediated by SpoIIAA, which reacts with the complex to cause the release of free sigmaF. Previous evidence indicated that Arg-20 in SpoIIAB is a contact site for both sigmaF and SpoIIAA and that contact with sigmaF is mediated by Arg-20 on only one of the two subunits in the sigmaF.SpoIIAB2 complex. Here we report the construction of heterodimers of SpoIIAB in which one subunit is wild type and the other subunit is a mutant for Arg-20. We show that the dissociation constant for the binding of sigmaF to the heterodimer was similar to that for the wild type, a finding consistent with the idea that sigmaF contacts Arg-20 on only one of the two subunits. Although SpoIIAA was highly effective in causing the release of sigmaF from the wild type homodimer, the anti-antisigma factor had little effect on the release of sigmaF from the heterodimer. This finding is consistent with a model in which SpoIIAA docks on the sigmaF.SpoIIAB2 complex, making contact with the subunit in which Arg-20 is not in contact with sigmaF. SpoIIAB is both an anti-sigmaF factor and a protein kinase that phosphorylates and thereby inactivates SpoIIAA. We show that SpoIIAA effectively displaces sigmaF from a complex of sigmaF with a mutant (SpoIIABR105A) that is impaired in the kinase function of SpoIIAB. This result shows that SpoIIAA-mediated displacement of sigmaF from SpoIIAB does not require concomitant phosphorylation of SpoIIAA.
    MeSH term(s) Bacillus subtilis/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Catalytic Domain ; Dimerization ; Kinetics ; Models, Molecular ; Mutation ; Phosphorylation ; Sigma Factor/metabolism ; Spores, Bacterial/metabolism ; Transcription Factors/metabolism
    Chemical Substances Bacterial Proteins ; Sigma Factor ; Transcription Factors ; spore-specific proteins, Bacillus ; sporulation-specific sigma factors
    Language English
    Publishing date 2003-04-03
    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.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M302305200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Genetic dissection of the sporulation protein SpoIIE and its role in asymmetric division in Bacillus subtilis.

    Carniol, Karen / Ben-Yehuda, Sigal / King, Nicole / Losick, Richard

    Journal of bacteriology

    2005  Volume 187, Issue 10, Page(s) 3511–3520

    Abstract: SpoIIE is a dual-function protein in Bacillus subtilis that contributes to the switch from medial to polar cell division during sporulation and is responsible for activating the cell-specific transcription factor sigma(F). SpoIIE consists of an N- ... ...

    Abstract SpoIIE is a dual-function protein in Bacillus subtilis that contributes to the switch from medial to polar cell division during sporulation and is responsible for activating the cell-specific transcription factor sigma(F). SpoIIE consists of an N-terminal domain with 10 membrane-spanning segments (region I), a C-terminal phosphatase domain (region III), and a central domain (region II) of uncertain function. To investigate the role of SpoIIE in polar division, we took advantage of a system for efficiently producing polar septa during growth in a SpoIIE-dependent manner using cells engineered to produce the sporulation protein in response to an inducer. The results show that regions II and III play a critical role in polar septum formation and that specific amino acid substitutions in those regions affect the abilities of SpoIIE both to promote polar division and to localize to the division machinery. Additionally, we show that neither the phosphatase function of SpoIIE nor the N-terminal, membrane-spanning region is needed for the switch to asymmetric division.
    MeSH term(s) Amino Acid Substitution ; Bacillus subtilis/cytology ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Cell Division/physiology ; Mutagenesis, Site-Directed ; Protein Structure, Tertiary ; Spores, Bacterial/genetics
    Chemical Substances Bacterial Proteins ; spore-specific proteins, Bacillus
    Language English
    Publishing date 2005-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; 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.187.10.3511-3520.2005
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  9. Article: Insulation of the sigmaF regulatory system in Bacillus subtilis.

    Carniol, Karen / Kim, Tae-Jong / Price, Chester W / Losick, Richard

    Journal of bacteriology

    2004  Volume 186, Issue 13, Page(s) 4390–4394

    Abstract: The transcription factors sigmaF and sigmaB are related RNA polymerase sigma factors that govern dissimilar networks of adaptation to stress conditions in Bacillus subtilis. The two factors are controlled by closely related regulatory pathways, involving ...

    Abstract The transcription factors sigmaF and sigmaB are related RNA polymerase sigma factors that govern dissimilar networks of adaptation to stress conditions in Bacillus subtilis. The two factors are controlled by closely related regulatory pathways, involving protein kinases and phosphatases. We report that insulation of the sigmaF pathway from the sigmaB pathway involves the integrated action of both the cognate kinase and the cognate phosphatase.
    MeSH term(s) Bacillus subtilis/physiology ; Bacterial Proteins/physiology ; Carrier Proteins/physiology ; Phosphorylation ; Sigma Factor/physiology ; Transcription, Genetic
    Chemical Substances Bacterial Proteins ; Carrier Proteins ; FliA protein, Bacteria ; RsbW protein, bacteria ; SigB protein, Bacteria ; Sigma Factor
    Language English
    Publishing date 2004-07
    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.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.186.13.4390-4394.2004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: High-quality draft genome sequences of 28 Enterococcus sp. isolates.

    Palmer, Kelli L / Carniol, Karen / Manson, Janet M / Heiman, David / Shea, Terry / Young, Sarah / Zeng, Qiandong / Gevers, Dirk / Feldgarden, Michael / Birren, Bruce / Gilmore, Michael S

    Journal of bacteriology

    2010  Volume 192, Issue 9, Page(s) 2469–2470

    Abstract: The enterococci are low-GC Gram-positive bacteria that have emerged as leading causes of hospital-acquired infection. They are also commensals of the gastrointestinal tract of healthy humans and most other animals with gastrointestinal flora and are ... ...

    Abstract The enterococci are low-GC Gram-positive bacteria that have emerged as leading causes of hospital-acquired infection. They are also commensals of the gastrointestinal tract of healthy humans and most other animals with gastrointestinal flora and are important for food fermentations. Here we report the availability of draft genome sequences for 28 enterococcal strains of diverse origin, including the species Enterococcus faecalis, E. faecium, E. casseliflavus, and E. gallinarum.
    MeSH term(s) Enterococcus/genetics ; Genome, Bacterial/genetics ; Molecular Sequence Data
    Language English
    Publishing date 2010-05
    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.00153-10
    Database MEDical Literature Analysis and Retrieval System OnLINE

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