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The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners
- Source :
- Molecular and Cellular Biology, Molecular and Cellular Biology, American Society for Microbiology, 2005, 25 (10), pp.4092-104. ⟨10.1128/MCB.25.10.4092-4104.2005⟩
- Publication Year :
- 2005
- Publisher :
- HAL CCSD, 2005.
-
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.
- 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
Subjects
Details
- Language :
- English
- ISSN :
- 02707306 and 10985549
- Database :
- OpenAIRE
- Journal :
- Molecular and Cellular Biology, Molecular and Cellular Biology, American Society for Microbiology, 2005, 25 (10), pp.4092-104. ⟨10.1128/MCB.25.10.4092-4104.2005⟩
- Accession number :
- edsair.doi.dedup.....ff999f17d75d6e984843fc1de7aa9037