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  1. Article: On a roll for new TRF targets.

    Reina, Jaime H / Hernandez, Nouria

    Genes & development

    2007  Volume 21, Issue 22, Page(s) 2855–2860

    MeSH term(s) Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Animals ; Drosophila/cytology ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila Proteins/chemistry ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; HeLa Cells ; Histones/genetics ; Humans ; Mice ; Models, Biological ; Neurofibromin 1/genetics ; Neurofibromin 1/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; TATA Box Binding Protein-Like Proteins/genetics ; TATA Box Binding Protein-Like Proteins/metabolism ; Telomeric Repeat Binding Protein 2/chemistry ; Telomeric Repeat Binding Protein 2/genetics ; Telomeric Repeat Binding Protein 2/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Xenopus Proteins/genetics ; Xenopus Proteins/metabolism
    Chemical Substances Dref protein, Drosophila ; Drosophila Proteins ; Histones ; ISWI protein ; Neurofibromin 1 ; Nuclear Proteins ; TATA Box Binding Protein-Like Proteins ; TBP-related factor, Drosophila ; TBPL2 protein, human ; TRF2 protein, Drosophila ; TRF3 protein, mouse ; Telomeric Repeat Binding Protein 2 ; Transcription Factors ; Xenopus Proteins ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2007-11-15
    Publishing country United States
    Document type Comment ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 806684-x
    ISSN 1549-5477 ; 0890-9369
    ISSN (online) 1549-5477
    ISSN 0890-9369
    DOI 10.1101/gad.1623207
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Ligands for pheromone-sensing neurons are not conformationally activated odorant binding proteins.

    Gomez-Diaz, Carolina / Reina, Jaime H / Cambillau, Christian / Benton, Richard

    PLoS biology

    2013  Volume 11, Issue 4, Page(s) e1001546

    Abstract: Pheromones form an essential chemical language of intraspecific communication in many animals. How olfactory systems recognize pheromonal signals with both sensitivity and specificity is not well understood. An important in vivo paradigm for this process ...

    Abstract Pheromones form an essential chemical language of intraspecific communication in many animals. How olfactory systems recognize pheromonal signals with both sensitivity and specificity is not well understood. An important in vivo paradigm for this process is the detection mechanism of the sex pheromone (Z)-11-octadecenyl acetate (cis-vaccenyl acetate [cVA]) in Drosophila melanogaster. cVA-evoked neuronal activation requires a secreted odorant binding protein, LUSH, the CD36-related transmembrane protein SNMP, and the odorant receptor OR67d. Crystallographic analysis has revealed that cVA-bound LUSH is conformationally distinct from apo (unliganded) LUSH. Recombinantly expressed mutant versions of LUSH predicted to enhance or diminish these structural changes produce corresponding alterations in spontaneous and/or cVA-evoked activity when infused into olfactory sensilla, leading to a model in which the ligand for pheromone receptors is not free cVA, but LUSH that is "conformationally activated" upon cVA binding. Here we present evidence that contradicts this model. First, we demonstrate that the same LUSH mutants expressed transgenically affect neither basal nor pheromone-evoked activity. Second, we compare the structures of apo LUSH, cVA/LUSH, and complexes of LUSH with non-pheromonal ligands and find no conformational property of cVA/LUSH that can explain its proposed unique activated state. Finally, we show that high concentrations of cVA can induce neuronal activity in the absence of LUSH, but not SNMP or OR67d. Our findings are not consistent with the model that the cVA/LUSH complex acts as the pheromone ligand, and suggest that pheromone molecules alone directly activate neuronal receptors.
    MeSH term(s) Acetates ; Action Potentials ; Amino Acid Substitution ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/physiology ; Ligands ; Male ; Mutagenesis, Site-Directed ; Neurons/physiology ; Oleic Acids/physiology ; Pheromones/physiology ; Protein Conformation ; Receptors, Cell Surface/metabolism ; Receptors, Odorant/chemistry ; Receptors, Odorant/genetics ; Receptors, Odorant/metabolism ; Receptors, Pheromone ; Sex Attractants/physiology ; Structural Homology, Protein
    Chemical Substances Acetates ; Drosophila Proteins ; Ligands ; Oleic Acids ; Or67d protein, Drosophila ; Pheromones ; Receptors, Cell Surface ; Receptors, Odorant ; Receptors, Pheromone ; Sex Attractants ; Snmp1 protein, Drosophila ; cis-vaccenyl acetate ; odorant-binding protein
    Language English
    Publishing date 2013-04-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.1001546
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    Zs.A 6193: Show issues Location:
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  3. Article ; Online: Maf1, a new player in the regulation of human RNA polymerase III transcription.

    Reina, Jaime H / Azzouz, Teldja N / Hernandez, Nouria

    PloS one

    2006  Volume 1, Page(s) e134

    Abstract: Background: Human RNA polymerase III (pol III) transcription is regulated by several factors, including the tumor suppressors P53 and Rb, and the proto-oncogene c-Myc. In yeast, which lacks these proteins, a central regulator of pol III transcription, ... ...

    Abstract Background: Human RNA polymerase III (pol III) transcription is regulated by several factors, including the tumor suppressors P53 and Rb, and the proto-oncogene c-Myc. In yeast, which lacks these proteins, a central regulator of pol III transcription, called Maf1, has been described. Maf1 is required for repression of pol III transcription in response to several signal transduction pathways and is broadly conserved in eukaryotes.
    Methodology/principal findings: We show that human endogenous Maf1 can be co-immunoprecipitated with pol III and associates in vitro with two pol III subunits, the largest subunit RPC1 and the alpha-like subunit RPAC2. Maf1 represses pol III transcription in vitro and in vivo and is required for maximal pol III repression after exposure to MMS or rapamycin, treatments that both lead to Maf1 dephosphorylation.
    Conclusions/significance: These data suggest that Maf1 is a major regulator of pol III transcription in human cells.
    MeSH term(s) Base Sequence ; Cell Line ; DNA Primers/genetics ; HeLa Cells ; Humans ; In Vitro Techniques ; Methyl Methanesulfonate/pharmacology ; Phosphorylation ; Promoter Regions, Genetic ; Protein Subunits ; RNA Interference ; RNA Polymerase I/genetics ; RNA Polymerase II/genetics ; RNA Polymerase III/chemistry ; RNA Polymerase III/genetics ; RNA Polymerase III/metabolism ; RNA Stability ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Transfer/genetics ; RNA, Transfer/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/antagonists & inhibitors ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; TATA-Binding Protein Associated Factors/metabolism ; Transcription, Genetic/drug effects
    Chemical Substances BRF1 protein, human ; DNA Primers ; MAF1 protein, human ; Protein Subunits ; RNA, Messenger ; Recombinant Fusion Proteins ; Repressor Proteins ; TATA-Binding Protein Associated Factors ; RNA, Transfer (9014-25-9) ; Methyl Methanesulfonate (AT5C31J09G) ; RNA Polymerase II (EC 2.7.7.-) ; RNA Polymerase I (EC 2.7.7.6) ; RNA Polymerase III (EC 2.7.7.6)
    Language English
    Publishing date 2006-12-27
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0000134
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  4. Article ; Online: Defining the RNA polymerase III transcriptome: Genome-wide localization of the RNA polymerase III transcription machinery in human cells.

    Canella, Donatella / Praz, Viviane / Reina, Jaime H / Cousin, Pascal / Hernandez, Nouria

    Genome research

    2010  Volume 20, Issue 6, Page(s) 710–721

    Abstract: Our view of the RNA polymerase III (Pol III) transcription machinery in mammalian cells arises mostly from studies of the RN5S (5S) gene, the Ad2 VAI gene, and the RNU6 (U6) gene, as paradigms for genes with type 1, 2, and 3 promoters. Recruitment of Pol ...

    Abstract Our view of the RNA polymerase III (Pol III) transcription machinery in mammalian cells arises mostly from studies of the RN5S (5S) gene, the Ad2 VAI gene, and the RNU6 (U6) gene, as paradigms for genes with type 1, 2, and 3 promoters. Recruitment of Pol III onto these genes requires prior binding of well-characterized transcription factors. Technical limitations in dealing with repeated genomic units, typically found at mammalian Pol III genes, have so far hampered genome-wide studies of the Pol III transcription machinery and transcriptome. We have localized, genome-wide, Pol III and some of its transcription factors. Our results reveal broad usage of the known Pol III transcription machinery and define a minimal Pol III transcriptome in dividing IMR90hTert fibroblasts. This transcriptome consists of some 500 actively transcribed genes including a few dozen candidate novel genes, of which we confirmed nine as Pol III transcription units by additional methods. It does not contain any of the microRNA genes previously described as transcribed by Pol III, but reveals two other microRNA genes, MIR886 (hsa-mir-886) and MIR1975 (RNY5, hY5, hsa-mir-1975), which are genuine Pol III transcription units.
    MeSH term(s) Base Sequence ; Gene Expression Profiling ; Genome, Human ; Humans ; Molecular Sequence Data ; RNA Polymerase III/genetics ; RNA, Transfer/genetics
    Chemical Substances RNA, Transfer (9014-25-9) ; RNA Polymerase III (EC 2.7.7.6)
    Language English
    Publishing date 2010-04-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1284872-4
    ISSN 1549-5469 ; 1088-9051 ; 1054-9803
    ISSN (online) 1549-5469
    ISSN 1088-9051 ; 1054-9803
    DOI 10.1101/gr.101337.109
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3729: Show issues Location:
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  5. Article ; Online: A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism.

    Gomez-Diaz, Carolina / Bargeton, Benoîte / Abuin, Liliane / Bukar, Natalia / Reina, Jaime H / Bartoi, Tudor / Graf, Marion / Ong, Huy / Ulbrich, Maximilian H / Masson, Jean-Francois / Benton, Richard

    Nature communications

    2016  Volume 7, Page(s) 11866

    Abstract: CD36 transmembrane proteins have diverse roles in lipid uptake, cell adhesion and pathogen sensing. Despite numerous in vitro studies, how they act in native cellular contexts is poorly understood. A Drosophila CD36 homologue, sensory neuron membrane ... ...

    Abstract CD36 transmembrane proteins have diverse roles in lipid uptake, cell adhesion and pathogen sensing. Despite numerous in vitro studies, how they act in native cellular contexts is poorly understood. A Drosophila CD36 homologue, sensory neuron membrane protein 1 (SNMP1), was previously shown to facilitate detection of lipid-derived pheromones by their cognate receptors in olfactory cilia. Here we investigate how SNMP1 functions in vivo. Structure-activity dissection demonstrates that SNMP1's ectodomain is essential, but intracellular and transmembrane domains dispensable, for cilia localization and pheromone-evoked responses. SNMP1 can be substituted by mammalian CD36, whose ectodomain can interact with insect pheromones. Homology modelling, using the mammalian LIMP-2 structure as template, reveals a putative tunnel in the SNMP1 ectodomain that is sufficiently large to accommodate pheromone molecules. Amino-acid substitutions predicted to block this tunnel diminish pheromone sensitivity. We propose a model in which SNMP1 funnels hydrophobic pheromones from the extracellular fluid to integral membrane receptors.
    MeSH term(s) Animals ; Animals, Genetically Modified ; CD36 Antigens/chemistry ; CD36 Antigens/metabolism ; Conserved Sequence/genetics ; Disulfides/metabolism ; Drosophila/metabolism ; Drosophila Proteins/chemistry ; Drosophila Proteins/metabolism ; Evolution, Molecular ; Glycosylation ; Models, Molecular ; Pheromones/metabolism ; Protein Domains ; Protein Transport ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/metabolism ; Structural Homology, Protein ; Structure-Activity Relationship
    Chemical Substances CD36 Antigens ; Disulfides ; Drosophila Proteins ; Pheromones ; Receptors, Cell Surface ; Snmp1 protein, Drosophila
    Language English
    Publishing date 2016-06-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/ncomms11866
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  6. Article ; Online: mTORC1 directly phosphorylates and regulates human MAF1.

    Michels, Annemieke A / Robitaille, Aaron M / Buczynski-Ruchonnet, Diane / Hodroj, Wassim / Reina, Jaime H / Hall, Michael N / Hernandez, Nouria

    Molecular and cellular biology

    2010  Volume 30, Issue 15, Page(s) 3749–3757

    Abstract: mTORC1 is a central regulator of growth in response to nutrient availability, but few direct targets have been identified. RNA polymerase (pol) III produces a number of essential RNA molecules involved in protein synthesis, RNA maturation, and other ... ...

    Abstract mTORC1 is a central regulator of growth in response to nutrient availability, but few direct targets have been identified. RNA polymerase (pol) III produces a number of essential RNA molecules involved in protein synthesis, RNA maturation, and other processes. Its activity is highly regulated, and deregulation can lead to cell transformation. The human phosphoprotein MAF1 becomes dephosphorylated and represses pol III transcription after various stresses, but neither the significance of the phosphorylations nor the kinase involved is known. We find that human MAF1 is absolutely required for pol III repression in response to serum starvation or TORC1 inhibition by rapamycin or Torin1. The protein is phosphorylated mainly on residues S60, S68, and S75, and this inhibits its pol III repression function. The responsible kinase is mTORC1, which phosphorylates MAF1 directly. Our results describe molecular mechanisms by which mTORC1 controls human MAF1, a key repressor of RNA polymerase III transcription, and add a new branch to the signal transduction cascade immediately downstream of TORC1.
    MeSH term(s) Humans ; Phosphorylation ; RNA Polymerase III/antagonists & inhibitors ; RNA Polymerase III/genetics ; RNA Polymerase III/metabolism ; Signal Transduction/drug effects ; Signal Transduction/genetics ; Sirolimus/metabolism ; Sirolimus/pharmacology ; Transfection
    Chemical Substances RNA Polymerase III (EC 2.7.7.6) ; Sirolimus (W36ZG6FT64)
    Language English
    Publishing date 2010-06-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00319-10
    Database MEDical Literature Analysis and Retrieval System OnLINE

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