Search

Your search keyword '"MESH: beta Karyopherins"' showing total 2 results
Start Over Descriptor "MESH: beta Karyopherins"
2 results on '"MESH: beta Karyopherins"'

1. TNPO3 Is Required for HIV-1 Replication after Nuclear Import but prior to Integration and Binds the HIV-1 Core

Author

Patricio Perez, Felipe Diaz-Griffero, Maritza Lienlaf, Abraham L. Brass, Jose Carlos Valle-Casuso, Yang Yang, Francesca Di Nunzio, Nathalie J. Arhel, Natalia Reszka, Department of Microbiology and Immunology, Albert Einstein College of Medicine [New York], Virologie moléculaire et vaccinologie, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Ragon Institute of Massachusetts General Hospital, Harvard Medical School [Boston] (HMS)-Massachusetts Institute of Technology (MIT), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Cell Nucleus, Cytoplasm, Virus Integration, Immunology, Human immunodeficiency virus (HIV), Active Transport, Cell Nucleus, HIV Infections, MESH: Active Transport, Cell Nucleus, Biology, medicine.disease_cause, Virus Replication, Microbiology, gag Gene Products, Human Immunodeficiency Virus, MESH: HIV-1, 03 medical and health sciences, Virology, medicine, MESH: Protein Binding, Humans, 030304 developmental biology, Cell Nucleus, 0303 health sciences, MESH: Humans, 030306 microbiology, MESH: Cytoplasm, MESH: Virus Replication, virus diseases, MESH: HIV Infections, beta Karyopherins, MESH: gag Gene Products, Human Immunodeficiency Virus, Replication (computing), 3. Good health, Virus-Cell Interactions, Core (game theory), Insect Science, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, HIV-1, Nuclear transport, MESH: beta Karyopherins, MESH: Virus Integration, Protein Binding
Abstract

TNPO3 is a nuclear importer required for HIV-1 infection. Here, we show that depletion of TNPO3 leads to an HIV-1 block after nuclear import but prior to integration. To investigate the mechanistic requirement of TNPO3 in HIV-1 infection, we tested the binding of TNPO3 to the HIV-1 core and found that TNPO3 binds to the HIV-1 core. Overall, this work suggests that TNPO3 interacts with the incoming HIV-1 core in the cytoplasm to assist a process that is important for HIV-1 infection after nuclear import.

Published
2012

2. The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners

Author

Elisabeth Scheer, Máté Á. Demény, Laszlo Tora, Giulia Fienga, Evi Soutoglou, Paolo Sassone-Corsi, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), and Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, Cytoplasm, Nuclear Localization Signals, Gene Expression, MESH: Nuclear Localization Signals, MESH: Spermatocytes, Diffusion, Histones, MESH: Protein Structure, Tertiary, 0302 clinical medicine, Spermatocytes, MESH: TATA-Binding Protein Associated Factors, MESH: Histones, 0303 health sciences, MESH: Transcription Factor TFIID, MESH: Diffusion, MESH: Transcription Factors, MESH: Fatty Acids, Unsaturated, beta Karyopherins, Cell biology, 030220 oncology & carcinogenesis, Fatty Acids, Unsaturated, Transcription factor II D, Protein Binding, MESH: Cell Nucleus, Active Transport, Cell Nucleus, Importin, MESH: Active Transport, Cell Nucleus, Biology, 03 medical and health sciences, Humans, MESH: Protein Binding, Molecular Biology, Transcription factor, 030304 developmental biology, Cell Nucleus, TATA-Binding Protein Associated Factors, MESH: Humans, TATA-Box Binding Protein, MESH: Cytoplasm, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Cell Biology, Molecular biology, MESH: Male, Protein Structure, Tertiary, MESH: Hela Cells, Transcription Factor TFIID, Nuclear transport, MESH: beta Karyopherins, Nuclear localization sequence, HeLa Cells, Transcription Factors
Abstract

International audience; TFIID, comprising the TATA box binding protein (TBP) and 13 TBP-associated factors (TAFs), plays a role in nucleation in the assembly of the RNA polymerase II preinitiation complexes on protein-encoding genes. TAFs are shared among other transcription regulatory complexes (e.g., SAGA, TBP-free TAF-containing complex [TFTC], STAGA, and PCAF/GCN5). Human TAF10, a subunit of both TFIID and TFTC, has three histone fold-containing interaction partners: TAF3, TAF8, and SPT7Like (SPT7L). In human cells, exogenously expressed TAF10 remains rather cytoplasmic and leptomycin B does not affect this localization. By using fluorescent fusion proteins, we show that TAF10 does not have an intrinsic nuclear localization signal (NLS) and needs one of its three interaction partners to be transported into the nucleus. When the NLS sequences of either TAF8 or SPT7L are mutated, TAF10 remains cytoplasmic, but a heterologous NLS can drive TAF10 into the nucleus. Experiments using fluorescence recovery after photobleaching show that TAF10 does not associate with any cytoplasmic partner but that once transported into the nucleus it binds to nuclear structures. TAF10 binding to importin beta in vitro is dependent on the coexpression of either TAF8 or TAF3, but not SPT7L. The cytoplasmic-nuclear transport of TAF10 is naturally observed during the differentiation of adult male germ cells. Thus, here we describe a novel role of the three mammalian interacting partners in the nuclear localization of TAF10, and our data suggest that a complex network of regulated cytoplasmic associations may exist among these factors and that this network is important for the composition of different TFIID and TFTC-type complexes in the nucleus.

Published
2005

Catalog

Books, media, physical & digital resources
See catalog results