Shige H. Yoshimura

Publication List Details

Period

2000 - 2008

Number

17

Co-Authors

Dynamic structures of Bacillus subtilis RecN–DNA complexes (2008)

Sánchez, Humberto, Cárdenas, Paula P., Yoshimura, Shige H., Takeyasu, Kunio, Alonso, Juan Carlos

Genetic and cytological evidences suggest that Bacillus subtilis RecN acts prior to and after endprocessing of DNA double-strand ends via homologous recombination, appears to participate in the...

Dynamic structures of Bacillus subtilis RecN-DNA complexes (2008)

Sanchez, Humberto, Cardenas, Paula P., Yoshimura, Shige H., Takeyasu, Kunio, Alonso, Juan C.

Genetic and cytological evidences suggest that Bacillus subtilis RecN acts prior to and after end-processing of DNA double-strand ends via homologous recombination, appears to participate in the...

Comparative structural biology of the genome: nano-scale imaging of single nucleus from different kingdoms reveals the common physicochemical property of chromatin with a 40 nm structural unit (2006)

Kobori, Toshiro, Kodama, Mami, Hizume, Kohji, Yoshimura, Shige H., Ohtani, Toshio, Takeyasu, Kunio

Genome function is closely linked to the higher-order chromatin structures. To reveal a structural basis for the interphase chromatin organization, the ‘on-substrate’ lysis procedure was applied...

Comparative structural biology of the genome: nano-scale imaging of single nucleus from different kingdoms reveals the common physicochemical property of chromatin with a 40 nm structural unit (2006)

Kobori, Toshiro, Kodama, Mami, Hizume, Kohji, Yoshimura, Shige H., Ohtani, Toshio, Takeyasu, Kunio

Genome function is closely linked to the higher-order chromatin structures. To reveal a structural basis for the interphase chromatin organization, the ‘on-substrate’ lysis procedure was applied...

Comparative structural biology of the genome: nano-scale imaging of single nucleus from different kingdoms reveals the common physicochemical property of chromatin with a 40 nm structural unit (2006)

Kobori, Toshiro, Kodama, Mami, Hizume, Kohji, Yoshimura, Shige H., Ohtani, Toshio, Takeyasu, Kunio

Genome function is closely linked to the higher-order chromatin structures. To reveal a structural basis for the interphase chromatin organization, the ‘on-substrate’ lysis procedure was applied...

Phase Transition in Reconstituted Chromatin (2004)

Nakai, Tonau, Hizume, Kohji, Yoshimura, Shige. H., Takeyasu, Kunio, Yoshikawa, Kenichi

By observing reconstituted chromatin by fluorescence microscopy (FM) and atomic force microscopy (AFM), we found that the density of nucleosomes exhibits a bimodal profile, i.e., there is a large...

Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy (2004)

Kim, Joongbaek, Yoshimura, Shige H., Hizume, Kohji, Ohniwa, Ryosuke L., Ishihama, Akira, Takeyasu, Kunio

A small container of several to a few hundred µm3 (i.e. bacterial cells and eukaryotic nuclei) contains extremely long genomic DNA (i.e. mm and m long, respectively) in a highly organized fashion....

On-substrate lysis treatment combined with scanning probe microscopy revealed chromosome structures in eukaryotes and prokaryotes (2003)

Yoshimura, Shige H., Kim, Joongbaek, Takeyasu, Kunio

The proper function of the genome largely depends on the higher‐order architecture of the chromosome. To understand the detailed chromosome structure in a native state, we developed an...

Atomic force microscopy proposes a 'kiss and pull' mechanism for enhancer function (2000)

Yoshimura, Shige H., Yoshida, Chikashi, Igarashi, Kazuhiko, Takeyasu, Kunio

The DNase I-hyper-sensitive sites (HS2–HS4) in the β-globin gene enhancer region (locus control region; LCR) have been known as the target of Bachl/MafK heterodimers. We have demonstrated...

Atomic force microscopy with carbon nanotube probe resolves the subunit organization of protein complexes (2000)

Hohmura, Ken I., Itokazu, Yutakatti, Yoshimura, Shige H., Mizuguchi, Gaku, Masamura, Yu-suke, Takeyasu, Kunio, ...

Among many scanning probe microscopies, atomic force microscopy (AFM) is a useful technique to analyse the structure of biological materials because of its applicability to non-conductors in...

Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy

Kim, Joongbaek, Yoshimura, Shige H., Hizume, Kohji, Ohniwa, Ryosuke L., Ishihama, Akira, Takeyasu, Kunio

A small container of several to a few hundred µm3 (i.e. bacterial cells and eukaryotic nuclei) contains extremely long genomic DNA (i.e. mm and m long, respectively) in a highly organized fashion....

Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy

Kim, Joongbaek, Yoshimura, Shige H., Hizume, Kohji, Ohniwa, Ryosuke L., Ishihama, Akira, Takeyasu, Kunio

A small container of several to a few hundred µm3 (i.e. bacterial cells and eukaryotic nuclei) contains extremely long genomic DNA (i.e. mm and m long, respectively) in a highly organized fashion....

Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL

Yokokawa, Masatoshi, Wada, Chieko, Ando, Toshio, Sakai, Nobuaki, Yagi, Akira, Yoshimura, Shige H, ...

In order to fold non-native proteins, chaperonin GroEL undergoes numerous conformational changes and GroES binding in the ATP-dependent reaction cycle. We constructed the real-time...

Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping

Crampton, Neal, Yokokawa, Masatoshi, Dryden, David T. F., Edwardson, J. Michael, Rao, Desirazu N., Takeyasu, Kunio, ...

Many DNA-modifying enzymes act in a manner that requires communication between two noncontiguous DNA sites. These sites can be brought into contact either by a diffusion-mediated chance interaction...

Dynamic structures of Bacillus subtilis RecN–DNA complexes

Sanchez, Humberto, Cardenas, Paula P., Yoshimura, Shige H., Takeyasu, Kunio, Alonso, Juan C.

Genetic and cytological evidences suggest that Bacillus subtilis RecN acts prior to and after end-processing of DNA double-strand ends via homologous recombination, appears to participate in the...

Individual binding pockets of importin-β for FG-nucleoporins have different binding properties and different sensitivities to RanGTP

Otsuka, Shotaro, Iwasaka, Shizuka, Yoneda, Yoshihiro, Takeyasu, Kunio, Yoshimura, Shige H.

Importin-β mediates protein transport across the nuclear envelope through the nuclear pore complex (NPC) by interacting with components of the NPC, called nucleoporins, and a small G protein, Ran....