FACT Facilitates Transcription-Dependent Nucleosome Alteration

• Published in: Science (American Association for the Advancement of Science) Vol. 301; no. 5636; pp. 1090 - 1093
• Main Authors: Belotserkovskaya, Rimma, Oh, Sangtaek, Bondarenko, Vladimir A., Orphanides, George, Studitsky, Vasily M., Reinberg, Danny
• Format: Journal Article
• Language: English
• Published: Washington, DC American Association for the Advancement of Science 22.08.2003; The American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Animals; Binding proteins; Biological and medical sciences; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - metabolism; Cell Line; Cells; Chromatin; Coding; Dimerization; Dimers; DNA; DNA - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Gels; Genes; Genetics; HeLa Cells; High Mobility Group Proteins - chemistry; High Mobility Group Proteins - metabolism; Histone chaperones; Histones; Histones - metabolism; Humans; Models, Genetic; Molecular and cellular biology; Molecular Chaperones - chemistry; Molecular Chaperones - metabolism; Molecular genetics; Molecular Sequence Data; Nucleosomes; Nucleosomes - metabolism; Physiological aspects; Protein Binding; Protein Subunits; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; RNA; RNA Polymerase II - metabolism; RNA polymerases; RNA synthesis; Synthesis; Templates, Genetic; Transcription Factors - chemistry; Transcription Factors - metabolism; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Transcriptional Elongation Factors - chemistry; Transcriptional Elongation Factors - metabolism; Yeasts; Nucleotidyltransferases; Enzyme; Transferases; Nucleosome; Molecular complex; Gene expression; Transcription factor; Histone; DNA-directed RNA polymerase; Elongation
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1085703

The FACT (facilitates chromatin transcription) complex is required for transcript elongation through nucleosomes by RNA polymerase II (Pol II) in vitro. Here, we show that FACT facilitates Pol II-driven transcription by destabilizing nu-cleosomal structure so that one histone H2A-H2B dimer is removed during enzyme passage. We also demonstrate that FACT possesses intrinsic histone chaperone activity and can deposit core histones onto DNA. Importantly, FACT activity requires both of its constituent subunits and is dependent on the highly acidic C terminus of its larger subunit, Spt16. These findings define the mechanism by which Pol II can transcribe through chromatin without disrupting its epigenetic status.