title: Crystal structure of elongator subcomplex Elp4-6.
abstract: Elongator is a multiprotein complex composed of two subcomplexes, Elp1-3 and Elp4-6. Elongator is highly conserved between yeast and humans and plays an important role in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. Here, we determined the crystal structure of the Elp4-6 subcomplex of yeast. The overall structure of Elp4-6 revealed that Elp6 acts as a bridge to assemble Elp4 and Elp5. Detailed structural and sequence analyses revealed that each subunit in the Elp4-6 subcomplex forms a RecA-ATPase-like fold, although it lacks the key sequence signature of ATPases. Site-directed mutagenesis and biochemical analyses indicated that the Elp4-6 subcomplex can assemble into a hexameric ring-shaped structure in vitro and in vivo. Furthermore, GST pulldown assays showed that the ring-shaped assembly of the Elp4-6 subcomplex is important for its specific histone H3 binding. Our results may shed light on the substrate recognition and assembly of the holo-Elongator complex.
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Zhijie
authors.initials: Z
authors.lastname: Lin
authors.forename: Weijing
authors.initials: W
authors.lastname: Zhao
authors.forename: Wentao
authors.initials: W
authors.lastname: Diao
authors.forename: Xingqiao
authors.initials: X
authors.lastname: Xie
authors.forename: Zheng
authors.initials: Z
authors.lastname: Wang
authors.forename: Jinxiu
authors.initials: J
authors.lastname: Zhang
authors.forename: Yuequan
authors.initials: Y
authors.lastname: Shen
authors.forename: Jiafu
authors.initials: J
authors.lastname: Long
mesh_terms: D018360:Crystallography, X-Ray; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D020836:Protein Structure, Quaternary; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: C571451:Elp4 protein, S cerevisiae; C571453:Elp6 protein, S cerevisiae; D046912:Multiprotein Complexes; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins