Publications by authors named "M Akatsu"
Article Synopsis
- The study focuses on H2A.B, a unique variant of the H2A histone, which plays important roles in processes like sperm and embryo development as well as cancer formation, pointing to its distinct transcriptional regulation compared to standard H2A.
- Researchers used solid-state nanopores to analyze how DNA unwinds from nucleosomes, discovering that H2A.B requires less voltage to completely unwind DNA and does so more rapidly than canonical H2A nucleosomes.
- The findings highlight that H2A.B facilitates a smoother DNA unwinding process due to quicker disassembly of the histone complex, suggesting a novel method for examining DNA-protein interactions and the dynamics of nucleosomes.
RNA polymerase II (RNAPII) transcribes DNA wrapped in the nucleosome by stepwise pausing, especially at nucleosomal superhelical locations -5 and -1 [SHL(-5) and SHL(-1), respectively]. In the present study, we performed cryo-electron microscopy analyses of RNAPII-nucleosome complexes paused at a major nucleosomal pausing site, SHL(-1). We determined two previously undetected structures, in which the transcribed DNA behind RNAPII is sharply kinked at the RNAPII exit tunnel and rewrapped around the nucleosomal histones in front of RNAPII by DNA looping.
View Article and Find Full Text PDFHistone H3.8 is a non-allelic human histone H3 variant derived from H3.3.
View Article and Find Full Text PDFThe N-terminal tails of histones protrude from the nucleosome core and are target sites for histone modifications, such as acetylation and methylation. Histone acetylation is considered to enhance transcription in chromatin. However, the contribution of the histone N-terminal tail to the nucleosome transcription by RNA polymerase II (RNAPII) has not been clarified.
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