Tomoko Migita
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Tomoko Migita has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Hiroshi Hashimoto
School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan
1 shared publication - Kazuhisa Kinoshita
Chromosome Dynamics Laboratory, RIKEN, Wako, Japan
1 shared publication - Kei Murakami
Department of Pharmaceutical Sciences, University of Shizuoka
1 shared publication - Kenichiro Shimizu
Department of Pharmaceutical Sciences, University of Shizuoka
1 shared publication - Kodai Hara
Department of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan
1 shared publication - Kozo Takeuchi
Chromosome Dynamics Laboratory, RIKEN
1 shared publication
Latest Publications
- Open Access
Structural basis of HEAT-kleisin interactions in the human condensin I subcomplex
ABSTRUCT: Condensin I is a multi-protein complex that plays an essential role in mitotic chromosome assembly and segregation in eukaryotes. It is composed of five subunits: two SMC (SMC2 and SMC4), a kleisin (CAP-H) and two HEAT-repeat (CAP-D2 and -G) subunits. Although it has been shown that balancing acts of the two HEAT-repeat subunits enable this complex to support dynamic assembly of chromosomal axes in vertebrate cells, its underlying mechanisms remain poorly understood. Here, we report the crystal structure of a human condensin I subcomplex comprising hCAP-G and hCAP-H. hCAP-H binds to the concave surfaces of a harp-shaped HEAT repeat domain of hCAP-G. A physical interaction between hCAP-G and hCAP-H is indeed essential for mitotic chromosome assembly recapitulated in Xenopus egg cell-free extracts. Furthermore, this study reveals that the human CAP-G-H subcomplex has the ability to interact with not only a double-stranded DNA, but also a single-stranded DNA, implicating potential, functional divergence of the vertebrate condensin I complex in mitotic chromosome assembly.
Open AccessStructural basis of HEAT-kleisin interactions in the human condensin I subcomplex
ABSTRUCT: Condensin I is a multi-protein complex that plays an essential role in mitotic chromosome assembly and segregation in eukaryotes. It is composed of five subunits: two SMC (SMC2 and SMC4), a kleisin (CAP-H) and two HEAT-repeat (CAP-D2 and -G) subunits. Although it has been shown that balancing acts of the two HEAT-repeat subunits enable this complex to support dynamic assembly of chromosomal axes in vertebrate cells, its underlying mechanisms remain poorly understood. Here, we report the crystal structure of a human condensin I subcomplex comprising hCAP-G and hCAP-H. hCAP-H binds to the concave surfaces of a harp-shaped HEAT repeat domain of hCAP-G. A physical interaction between hCAP-G and hCAP-H is indeed essential for mitotic chromosome assembly recapitulated in Xenopus egg cell-free extracts. Furthermore, this study reveals that the human CAP-G-H subcomplex has the ability to interact with not only a double-stranded DNA, but also a single-stranded DNA, implicating potential, functional divergence of the vertebrate condensin I complex in mitotic chromosome assembly.