Solution structure of the SWIRM domain of human histone demethylase LSD1.
SWIRM is an evolutionarily conserved domain involved in several chromatin-modifying complexes. Recently, the LSD1 protein, which bears a SWIRM domain, was found to be a demethylase for Lys4-methylated histone H3. Here, we report a solution structure of the SWIRM domain of human LSD1. It forms a compact fold composed of 6 alpha helices, in which a 20 amino acid long helix (alpha4) is surrounded by 5 other short helices. The SWIRM domain structure could be divided into the N-terminal part (alpha1-alpha3) and the C-terminal part (alpha4-alpha6), which are connected to each other by a salt bridge. While the N-terminal part forms a SWIRM-specific structure, the C-terminal part adopts a helix-turn-helix (HTH)-related fold. We discuss a model in which the SWIRM domain acts as an anchor site for a histone tail.
Tochio
Naoya
N
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Umehara
Takashi
T
Koshiba
Seizo
S
Inoue
Makoto
M
Yabuki
Takashi
T
Aoki
Masaaki
M
Seki
Eiko
E
Watanabe
Satoru
S
Tomo
Yasuko
Y
Hanada
Masaru
M
Ikari
Masaomi
M
Sato
Miyuki
M
Terada
Takaho
T
Nagase
Takahiro
T
Ohara
Osamu
O
Shirouzu
Mikako
M
Tanaka
Akiko
A
Kigawa
Takanori
T
Yokoyama
Shigeyuki
S
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D042002:Chromatin Assembly and Disassembly; D004268:DNA-Binding Proteins; D019077:Helix-Turn-Helix Motifs; D056466:Histone Demethylases; D006657:Histones / Q000032:analysis / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010089:Oxidoreductases, N-Demethylating / Q000737:chemistry / Q000235:genetics*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D013997:Time Factors; D014157:Transcription Factors / Q000032:analysis / Q000737:chemistry*
D004268:DNA-Binding Proteins; D006657:Histones; D014157:Transcription Factors; D056466:Histone Demethylases; C495195:KDM1A protein, human; D010089:Oxidoreductases, N-Demethylating