title: Structural features of the single-stranded DNA-binding protein MoSub1 from Magnaporthe oryzae.
abstract: The well studied general transcription cofactor Sub1/PC4 has multiple functions in transcription. It plays both a negative and a positive role in transcription initiation and is involved in elongation and downstream transcription processes and as a transcription reinitiation factor. MoSub1, a Sub1/PC4 orthologue from rice blast fungus, binds the single-stranded DNA dT(12) tightly with an affinity of 186 nM. The crystal structure of MoSub1 has been solved to 1.79 Å resolution. The structure of the protein shows high similiarity to the structure of PC4 and it has a similar dimer interface and DNA-binding region to PC4, indicating that MoSub1 could bind DNA using the same motif as other proteins of the Sub1/PC4 family. There are two novel features in the MoSub1 structure: a region N-terminal to the DNA-binding domain and a C-terminal extension. The region N-terminal to the DNA-binding domain of MoSub1 turns back towards the DNA-binding site and may interact directly with DNA or the DNA-binding site. The C-terminal extension region, which is absent in PC4, may not be capable of interacting with DNA and is one possible reason for the differences between Sub1 and PC4.
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, People's Republic of China.
authors.forename: Jinguang
authors.initials: J
authors.lastname: Huang
authors.forename: Yanxiang
authors.initials: Y
authors.lastname: Zhao
authors.forename: Dan
authors.initials: D
authors.lastname: Huang
authors.forename: Huaian
authors.initials: H
authors.lastname: Liu
authors.forename: Neil
authors.initials: N
authors.lastname: Justin
authors.forename: Wensheng
authors.initials: W
authors.lastname: Zhao
authors.forename: Junfeng
authors.initials: J
authors.lastname: Liu
authors.forename: Youliang
authors.initials: Y
authors.lastname: Peng
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D020082:Magnaporthe / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D004268:DNA-Binding Proteins