Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules

Nature Communications

Volumn 6, Issue , 2015, Pages

  Trowitzsch, Simon ^a   Viola, Cristina ^a   Scheer, Elisabeth ^b   Conic, Sascha ^b   Chavant, Virginie ^b   Fournier, Marjorie ^b   Papai, Gabor ^b   Ebong, Ima Obong ^c   Schaffitzel, Christiane ^a   Zou, Juan ^d   Haffke, Matthias ^a   Rappsilber, Juri ^d,e   Robinson, Carol V ^c   Schultz, Patrick ^b   Tora, Laszlo ^b   Berger, Imre ^a,f  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^b INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d UNIVERSITY OF EDINBURGH   (United Kingdom)

^e TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^f UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GENERAL TRANSCRIPTION FACTOR; HISTONE; TATA BINDING PROTEIN; TATA BINDING PROTEIN ASSOCIATED FACTOR; TRANSCRIPTION FACTOR; PROTEIN BINDING; RECOMBINANT PROTEIN; SUPT7L PROTEIN, HUMAN; TAF10 PROTEIN, HUMAN; TAF2 PROTEIN, HUMAN; TAF8 PROTEIN, HUMAN; TRANSCRIPTION FACTOR IID;

CYTOLOGY; CYTOPLASM; EUKARYOTE; MASS SPECTROMETRY; PROTEIN;

ARTICLE; CELL NUCLEUS; COMPLEX FORMATION; CYTOPLASM; HUMAN; HUMAN CELL; MASS SPECTROMETRY; NONHUMAN; NUCLEAR IMPORT; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MOTIF; X RAY CRYSTALLOGRAPHY; CALORIMETRY; CHEMISTRY; HELA CELL LINE; METABOLISM; MOLECULAR MODEL; PROCEDURES; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SURFACE PLASMON RESONANCE;

EUKARYOTA;

AMINO ACID MOTIFS; CALORIMETRY; CELL NUCLEUS; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; HELA CELLS; HISTONES; HUMANS; MASS SPECTROMETRY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SURFACE PLASMON RESONANCE; TATA-BINDING PROTEIN ASSOCIATED FACTORS; TRANSCRIPTION FACTOR TFIID; TRANSCRIPTION FACTORS;

EID: 84923073621     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7011     Document Type: Article

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