TY - JOUR
T1 - Structural and Functional Differences of SWIRM Domain Subtypes
AU - Yoneyama, Misao
AU - Tochio, Naoya
AU - Umehara, Takashi
AU - Koshiba, Seizo
AU - Inoue, Makoto
AU - Yabuki, Takashi
AU - Aoki, Masaaki
AU - Seki, Eiko
AU - Matsuda, Takayoshi
AU - Watanabe, Satoru
AU - Tomo, Yasuko
AU - Nishimura, Yuji
AU - Harada, Takushi
AU - Terada, Takaho
AU - Shirouzu, Mikako
AU - Hayashizaki, Yoshihide
AU - Ohara, Osamu
AU - Tanaka, Akiko
AU - Kigawa, Takanori
AU - Yokoyama, Shigeyuki
N1 - Funding Information:
We thank Yukiko Fujikura, Natsuko Matsuda, Natsumi Suzuki, Yoko Motoda, Yukako Miyata, Atsuo Kobayashi, Kazuharu Hanada, Masaomi Ikari, Fumiko Hiroyasu, Miyuki Sato, Yuri Tsuboi, Tomomi Ide, Yuki Kamewari, Naomi Obayashi, Hiroaki Hamana, Nobuko Maoka, and Masatoshi Wakamori for sample preparation, and Tomoko Nakayama, Kiyomi Yajima, Azusa Ishii, and Mitsue Sunada for clerical assistance. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI), the National Project on Protein Structural and Functional Analyses, Ministry of Education, Culture, Sports, Science and Technology of Japan.
PY - 2007/5/25
Y1 - 2007/5/25
N2 - SWIRM is a conserved domain found in several chromatin-associated proteins. Based on their sequences, the SWIRM family members can be classified into three subfamilies, which are represented by Swi3, LSD1, and Ada2. Here we report the SWIRM structure of human MYb-like, Swirm and Mpn domain-containing protein-1 (MYSM1). The MYSM1 SWIRM structure forms a compact HTH-related fold comprising five α-helices, which best resembles the Swi3 SWIRM structure, among the known SWIRM structures. The MYSM1 and Swi3 SWIRM structures are more similar to the LSD1 structure than the Ada2α structure. The SWIRM domains of MYSM1 and LSD1 lacked DNA binding activity, while those of Ada2α and the human Swi3 counterpart, SMARCC2, bound DNA. The dissimilarity in the DNA-binding ability of the MYSM1 and SMARCC2 SWIRM domains might be due to a couple of amino acid differences in the last helix. These results indicate that the SWIRM family has indeed diverged into three structural subfamilies (Swi3/MYSM1, LSD1, and Ada2 types), and that the Swi3/MYSM1-type subfamily has further diverged into two functionally distinct groups. We also solved the structure of the SANT domain of MYSM1, and demonstrated that it bound DNA with a similar mode to that of the c-Myb DNA-binding domain.
AB - SWIRM is a conserved domain found in several chromatin-associated proteins. Based on their sequences, the SWIRM family members can be classified into three subfamilies, which are represented by Swi3, LSD1, and Ada2. Here we report the SWIRM structure of human MYb-like, Swirm and Mpn domain-containing protein-1 (MYSM1). The MYSM1 SWIRM structure forms a compact HTH-related fold comprising five α-helices, which best resembles the Swi3 SWIRM structure, among the known SWIRM structures. The MYSM1 and Swi3 SWIRM structures are more similar to the LSD1 structure than the Ada2α structure. The SWIRM domains of MYSM1 and LSD1 lacked DNA binding activity, while those of Ada2α and the human Swi3 counterpart, SMARCC2, bound DNA. The dissimilarity in the DNA-binding ability of the MYSM1 and SMARCC2 SWIRM domains might be due to a couple of amino acid differences in the last helix. These results indicate that the SWIRM family has indeed diverged into three structural subfamilies (Swi3/MYSM1, LSD1, and Ada2 types), and that the Swi3/MYSM1-type subfamily has further diverged into two functionally distinct groups. We also solved the structure of the SANT domain of MYSM1, and demonstrated that it bound DNA with a similar mode to that of the c-Myb DNA-binding domain.
KW - Pfam
KW - chromatin
KW - evolution
KW - histone
KW - solution structure
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U2 - 10.1016/j.jmb.2007.03.027
DO - 10.1016/j.jmb.2007.03.027
M3 - Article
C2 - 17428495
AN - SCOPUS:34247390658
VL - 369
SP - 222
EP - 238
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -