scholarly journals Separate-type scanner and wideband high-voltage amplifier for atomic-resolution and high-speed atomic force microscopy

2013 ◽  
Vol 84 (4) ◽  
pp. 043705 ◽  
Author(s):  
Kazuki Miyata ◽  
Satoshi Usho ◽  
Satoshi Yamada ◽  
Shoji Furuya ◽  
Kiyonori Yoshida ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
High Voltage ◽  
High Speed ◽  
Atomic Resolution ◽  
Force Microscopy ◽  
Separate Type ◽  
Atomic Force ◽  
Voltage Amplifier

scholarly journals Note: High-speed Z tip scanner with screw cantilever holding mechanism for atomic-resolution atomic force microscopy in liquid

2014 ◽  
Vol 85 (12) ◽  
pp. 126106 ◽  
Author(s):  
Seyed Mohammad Reza Akrami ◽  
Kazuki Miyata ◽  
Hitoshi Asakawa ◽  
Takeshi Fukuma
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Atomic Resolution ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Rina Hirano ◽  
Yasuhiro Arimura ◽  
Tomoya Kujirai ◽  
Mikihiro Shibata ◽  
Aya Okuda ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Dna Repair ◽  
High Speed ◽  
Histone Chaperones ◽  
Histone H2a ◽  
Force Microscopy ◽  
Atomic Force ◽  
Open Conformation ◽  
Replication Sites ◽  
Histone Exchange

AbstractH2A.B is an evolutionarily distant histone H2A variant that accumulates on DNA repair sites, DNA replication sites, and actively transcribing regions in genomes. In cells, H2A.B exchanges rapidly in chromatin, but the mechanism has remained enigmatic. In the present study, we found that the H2A.B-H2B dimer incorporated within the nucleosome exchanges with the canonical H2A-H2B dimer without assistance from additional factors, such as histone chaperones and nucleosome remodelers. High-speed atomic force microscopy revealed that the H2A.B nucleosome, but not the canonical H2A nucleosome, transiently forms an intermediate “open conformation”, in which two H2A.B-H2B dimers may be detached from the H3-H4 tetramer and bind to the DNA regions near the entry/exit sites. Mutational analyses revealed that the H2A.B C-terminal region is responsible for the adoption of the open conformation and the H2A.B-H2B exchange in the nucleosome. These findings provide mechanistic insights into the histone exchange of the H2A.B nucleosome.

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