TAKAMI Yasunari

写真a

Affiliation

Faculty of Medicine School of Medicine Department of Medical Sciences, Biochemistry and Molecular Biology

Title

Associate Professor

External Link

Degree 【 display / non-display

  • 医学博士 ( 1991.3   大阪大学 )

  • 農学修士 ( 1987.3   大阪府立大学 )

Research Areas 【 display / non-display

  • Life Science / Genome biology  / molecular biology

  • Life Science / Molecular biology  / molecular biology

 

Papers 【 display / non-display

  • Role of cytoplasmic acetyltransferases, NAA60 and HAT1, in cellular protection against genotoxic agents Reviewed International coauthorship

    Satrimafitrah Pasjan, Nishitoh Hideki, Takami Yasunari

    Fundamental Toxicological Sciences   9 ( 6 )   179 - 186   2022

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    Authorship:Last author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:一般社団法人 日本毒性学会  

    Histone acetyltransferases (HATs) are separated into two types. Type A HATs act on nucleosomal histones and thus primarily function in transcriptional regulation, while cytoplasmic HATs (type B) are known as enzymes that modify free histones before their assembly into chromatin, and may also function outside the nucleus. N-alpha-acetyltransferase 60 (NAA60) is the most recently discovered type B HATs, which are also known as N-terminal acetyltransferases (NATs) and are found only in multicellular eukaryotes. NAA60 localizes to the Golgi complex and possesses a unique ability to catalyze the acetylation of membrane-anchored proteins at the N-terminus and free histones at the lysine side chains, the biological significance of which remains unclear. To investigate the cellular functions of NAA60 and its relation to other cytoplasmic HATs, Hat1, we generated <i>NAA60-</i> or <i>HAT1-</i>deficient cells and <i>NAA60/HAT1-</i>double deficient cells using a chicken B lymphocyte leukemia DT40 cell line. Although NAA60-deficient cells did not show any impairment in cell growth and showed a slight sensitivity to DNA damage agents, <i>NAA60/HAT1-</i>double deficient cells exhibited an additive increase in sensitivity to methyl methanesulfonate (MMS) and 4-nitroquinoline 1-oxide (4-NQO) when compared to <i>HAT1-</i>deficient cells, which were previously reported to be moderately sensitive to these agents. These results predict that each type B HATs might contribute differently in regulation of repair of chemical induced DNA lesions.

    DOI: 10.2131/fts.9.179

    CiNii Research

  • Histone H1 quantity determines the efficiency of chromatin condensation in both apoptotic and live cells Reviewed

    Kijima M., Yamagishi H., Hara Y., Kasai M., Takami Y., Takemura H., Miyanari Y., Shinkai Y., Mizuta R.

    Biochemical and Biophysical Research Communications   512 ( 2 )   202 - 207   2019

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Biochemical and Biophysical Research Communications  

    © 2019 Elsevier Inc. Although chromatin condensation is a well-known hallmark of apoptosis, the generation mechanism has not been clarified. Histone H1, a positively-charged abundant nuclear protein, is located in the linker region of chromatin. There are several Histone H1 subtypes that are encoded by variant genes. Using serial histone H1-deletion mutant cells established from the chicken B-cell leukemia line DT40, we found that apoptotic chromatin condensation was decreased in relation to histone H1 protein level and that the chromatin in nuclei prepared from the live null mutant cells had a high accessibility of DNases and transposase. This indicated that linker histone H1 was the general chromatin condensation factor and that the loss of histone H1 generated open chromatin in both apoptotic and live cells.

    DOI: 10.1016/j.bbrc.2019.03.030

    Scopus

    PubMed

  • Molecular mechanism of ER stress-induced pre-emptive quality control involving association of the translocon, Derlin-1, and HRD1 Reviewed

    Kadowaki H., Satrimafitrah P., Takami Y., Nishitoh H.

    Scientific Reports   8 ( 1 )   7317   2018.12

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Scientific Reports  

    © 2018 The Author(s). The maintenance of endoplasmic reticulum (ER) homeostasis is essential for cell function. ER stress-induced pre-emptive quality control (ERpQC) helps alleviate the burden to a stressed ER by limiting further protein loading. We have previously reported the mechanisms of ERpQC, which includes a rerouting step and a degradation step. Under ER stress conditions, Derlin family proteins (Derlins), which are components of ER-associated degradation, reroute specific ER-targeting proteins to the cytosol. Newly synthesized rerouted polypeptides are degraded via the cytosolic chaperone Bag6 and the AAA-ATPase p97 in the ubiquitin-proteasome system. However, the mechanisms by which ER-targeting proteins are rerouted from the ER translocation pathway to the cytosolic degradation pathway and how the E3 ligase ubiquitinates ERpQC substrates remain unclear. Here, we show that ERpQC substrates are captured by the carboxyl-terminus region of Derlin-1 and ubiquitinated by the HRD1 E3 ubiquitin ligase prior to degradation. Moreover, HRD1 forms a large ERpQC-related complex composed of Sec61α and Derlin-1 during ER stress. These findings indicate that the association of the degradation factor HRD1 with the translocon and the rerouting factor Derlin-1 may be necessary for the smooth and effective clearance of ERpQC substrates.

    DOI: 10.1038/s41598-018-25724-x

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  • Acetylation of histone H4 lysine 5 and 12 is required for CENP-A deposition into centromeres. Reviewed

    Wei-Hao Shang, Tetsuya Hori, Frederick G. Westhorpe, Kristina M. Godek, Atsushi Toyoda, Sadahiko Misu, Norikazu Monma, Kazuho Ikeo, Christopher W. Carroll, Yasunari Takami, Asao Fujiyama, Hiroshi Kimura, Aaron F. Straight, Tatsuo Fukagawa

    Nature Communications   7 ( 13465 )   1 - 13   2016.11

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/ncomms13465

  • RbAp48 is essential for viability of vertebrate cells and plays a role in chromosome stability Reviewed

    Satrimafitrah P, Barman HK, Ahmad A, Nishitoh H, Nakayama T, Fukagawa T, Takami Y

    Chromosome Research   24 ( 2 )   161 - 173   2016.5

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1007/s10577-015-9510-8

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Books 【 display / non-display

  • Advances in Genetics Research vol.2. (Studies on epigenetic control of B cell functions using the DT40 cell line)

    Hidehiko Kikuchi, Hirak Kumar Barman, Masami Nakayama, Yasunari Takami, Tatsuo Nakayama( Role: Joint author)

    Urbano (Ed). Nova Science Publishers  2010.3 

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    Language:English Book type:Scholarly book

  • Reviews and Protocol in DT40 Research

    Kikuchi H., Barman H K., Nakayama M., Takami Y., and Nakayama T.( Role: Joint author ,  部分執筆)

    Springer-Verlag (Verlin)  2006.4 

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    Language:English Book type:Scholarly book

MISC 【 display / non-display

  • Regulation of DNA replication through chromatin assembly

    Yasunari Takami

    PUROTEIN. NUCLEIC ACID, ENZYME   54 ( 4 )   496 - 501   2009.4

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (trade magazine, newspaper, online media)  

  • Participation of histones and histone-modifying enzymes in cell functions through alterations in chromatin structure.

    Nakayama T., and Takami Y.

    Journal of Biochemistry   29   491 - 499   2001.4

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    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:Journal of Biochemistry  

Presentations 【 display / non-display

  • RbAp48 is essential for the viability and plays a role for chromosome stability in vertebrate Cells

    Pasjan Satrimafitrah, Hirak Kumar Barman, Ahyar Ahmad , Hideki Nishitoh, Tatsuo Nakayama, Tatsuo Fukagawa, Yasunari Takami

    平成27年度日本生化学会九州支部会  (九州大学箱崎 キャンパス)  日本生化学会九州支部

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    Event date: 2015.5.16 - 2015.5.17

    Language:English   Presentation type:Oral presentation (general)  

    Venue:九州大学箱崎 キャンパス  

  • RbAp48 is essential for the viability and plays a role for chromosome stability in vertebrate Cells International conference

    Pasjan Satrimafitrah, Hirak Kumar Barman, Ahyar Ahmad , Hideki Nishitoh, Tatsuo Nakayama, Tatsuo Fukagawa, Yasunari Takami

    平成27年度日本生化学会九州支部会  (九州大学箱崎 キャンパス)  日本生化学会九州支部

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    Event date: 2015.5.16

    Language:Japanese  

    Venue:九州大学箱崎 キャンパス  

  • Protective role of Naa60, a cellular acetyltransferase, in chemically induced DN A damage

    Pasjan Satrima Fitrah, Hideki Nishitoh, Yasunari Takami

    第37回日本分子生物学会年会  (パシフィコ横浜)  日本分子生物学会

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    Event date: 2014.11.25 - 2014.11.27

    Language:English   Presentation type:Poster presentation  

    Venue:パシフィコ横浜  

  • The biological function of the WD40 repeat-containing protein RbAp48 in DT40 cells

    Yasunari Takami, Pasjan S Fitrah, Tatsuo Nakayama, Hideki Nishitoh

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    Event date: 2013.12.3 - 2013.12.6

    Language:Japanese   Presentation type:Poster presentation  

  • ヒストンシャペロンRbAp48はCAF-1活性と可溶性H3-H4複合体の動態を制御する

    高見恭成, Pasjan Satrima Fitrah, 西頭英起

    第37回 蛋白質と酵素の構造と機能に関する九州シンポジウム  (長崎県雲仙市)  蛋白質と酵素の構造と機能に関する九州シンポジウム

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    Event date: 2013.9.26 - 2013.9.28

    Language:Japanese   Presentation type:Poster presentation  

    Venue:長崎県雲仙市  

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Grant-in-Aid for Scientific Research 【 display / non-display

  • ゲノム改変細胞を用いたコアヒストンの生理機能解析

    Grant number: 18K06186  2018.04 - 2021.03

    科学研究費補助金  基盤研究(C)

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    Authorship:Principal investigator 

  • ゲノム損傷応答修復機構におけるヒストン修飾とクロマチン制御因子の役割

    2014.04 - 2017.03

    科学研究費補助金  基盤研究(C)

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    Authorship:Principal investigator 

    ゲノム損傷応答修復機構におけるヒストン修飾とクロマチン制御因子の役割

  • DNA複製に共役したクロマチン形成機構と組換えー修復機構の関連

    2009.04 - 2012.03

    科学研究費補助金  基盤研究(C)

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    Authorship:Principal investigator 

    DNA複製に共役したクロマチン形成機構と組換えー修復機構の関連

  • 自己免疫とRNA修飾:全身性エリテマトーデス発症の分子機構

    2009.04 - 2010.03

    科学研究費補助金  特定領域研究

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    Authorship:Coinvestigator(s) 

    タンパク質に翻訳されないノンコーディングRNA(ncRNA)が、生体内に多数存在する。これらのRNAは種々の修飾を受けているが、その意義は不明である。一方、全身性エリテマトーデス(SLE)患者の血清からリボソームRNAに対する抗体が多数見つかっている。なぜこのような抗体ができるのかは明らかではない。私たちは、RNA修飾の有無が免疫活性化の原因になるのではないかと考えた。これを明らかにするために、修飾欠損モデルを作製し、生体システムにおけるRNA修飾の役割を分子レベルで解析した。

  • ゲノム損傷応答修復機構におけるクロマチン制御因子の役割

    2008.04 - 2010.03

    科学研究費補助金  特定領域研究

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    Authorship:Principal investigator 

    ゲノム損傷応答修復機構におけるクロマチン制御因子の役割

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