title: Solution structure of the Taf14 YEATS domain and its roles in cell growth of Saccharomyces cerevisiae.
abstract: Chromatin modifications play important roles in cellular biological process. A novel conserved domain family, YEATS, has been discovered in a variety of eukaryotic species ranging from yeasts to humans. Taf14, which is involved in a few protein complexes of chromatin remodelling and gene transcription, and is essential for keeping chromosome stability, regular cell growth and transcriptional regulation, contains a YEATS domain at its N-terminus. In the present study, we determined the solution structure of the Taf14 YEATS domain using NMR spectroscopy. The Taf14 YEATS domain adopts a global fold of an elongated β-sandwich, similar to the Yaf9 YEATS domain. However, the Taf14 YEATS domain differs significantly from the Yaf9 YEATS domain in some aspects, which might indicate different structural classes of the YEATS domain family. Functional studies indicate that the YEATS domain is critical for the function of Taf14 in inhibiting cell growth under stress conditions. In addition, our results show that the C-terminus of Taf14 is responsible for its interaction with Sth1, which is an essential component of the RSC complex. Taken together, this implies that Taf14 is involved in transcriptional activation of Saccharomyces cerevisiae and the YEATS domain of Taf14 might play a negative role in cell growth.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026, China.
authors.forename: Wen
authors.initials: W
authors.lastname: Zhang
authors.forename: Jiahai
authors.initials: J
authors.lastname: Zhang
authors.forename: Xuecheng
authors.initials: X
authors.lastname: Zhang
authors.forename: Chao
authors.initials: C
authors.lastname: Xu
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Tu
mesh_terms: D000595:Amino Acid Sequence; D042002:Chromatin Assembly and Disassembly; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000254:growth & development* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D035362:Transcription Factor TFIID / Q000737:chemistry* / Q000378:metabolism; D015533:Transcriptional Activation
chemical_list: D029701:Saccharomyces cerevisiae Proteins; C090313:TAF14 protein, S cerevisiae; D035362:Transcription Factor TFIID; C477280:YAF9 protein, S cerevisiae; D051548:Histone Acetyltransferases