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Yoshito Abe Last modified date:2020.02.26

Associate Professor / Department of Bio-Pharmaceutical Sciences
Department of Pharmaceutical Health Care and Sciences
Faculty of Pharmaceutical Sciences

Other Organization

Our group, the Immunology Laboratory, is involved in a number of areas: Structural Biology, Protein engineering and Immunology.
In the web, our publication, research, and activity were described. .
Academic Degree
ph. D
Country of degree conferring institution (Overseas)
Field of Specialization
protein chemistry, structural biology
Total Priod of education and research career in the foreign country
Outline Activities
My research is the analysis of protein structure and function based on protein chemistry, structual biology.

DNA replication restart, AL amyloidosis, anti-P2X4 antibody.

Biochemistry based on proteins.
Research Interests
  • Study in mechanism for retardation of amyloid formation
    keyword : Protein engineering、Protein chemistry
  • structure and function of invertebrate type lysozyme
    keyword : Structure biology, protein engineering
  • Structure and function of DNA replication initiation protein in Escherichia coli
    keyword : Structure biology, protein engineering
  • Structure and function of memebrane protein
    keyword : Structure biology, protein engineering
Academic Activities
1. Saki Fujiyama, Yoshito Abe, Mitsunori Shiroishi, Yohei Ikeda, Tadashi Ueda, Insight into the interaction between PriB and DnaT on bacterial DNA replication restart
Significance of the residues on PriB dimer interface and highly acidic region on DnaT, Biochimica et Biophysica Acta - Proteins and Proteomics, 10.1016/j.bbapap.2019.01.008, 1867, 4, 367-375, 2019.01, When the replisome collapses at a DNA damage site, a sequence-independent replication restart system is required. In Escherichia coli, PriA, PriB, and DnaT assemble in an orderly fashion at the stalled replication fork and achieve the reloading of the replisome. PriB-DnaT interaction is considered a significant step in the replication restart. In this study, we examined the contribution of the residues Ser20, His26 and Ser55, which are located on the PriB dimer interface. These residues are proximal to Glu39 and Arg44, which are important for PriB-DnaT interaction. Mutational analyses revealed that His26 and Ser20 of PriB are important for the interaction with DnaT, and that the Ser55 residue of PriB might have a role in negatively regulating the DnaT binding. These residues are involved in not only the interaction between PriB and DnaT but also the dissociation of single-stranded DNA (ssDNA) from the PriB-ssDNA complex due to DnaT binding. Moreover, NMR study indicates that the region Asp66-Glu76 on the linker between DnaT domains is involved in the interaction with wild-type PriB. These findings provide significant information about the molecular mechanism underlying replication restart in bacteria..
2. Tatsuhiro Igawa, Shuhei Kishikawa, Yoshito Abe, Tomohiro Yamashita, Saki Nagai, Mitsunori Shiroishi, Chinatsu Shinozaki, Hiroyuki Tanaka, Hidetoshi Tozaki-Saitoh, Makoto Tsuda, Kazuhide Inoue, Tadashi Ueda, Evidence for detection of rat P2X4 receptor expressed on cells by generating monoclonal antibodies recognizing the native structure, Purinergic Signalling, 10.1007/s11302-019-09646-5, 2019.01, P2X purinergic receptors are ATP-driven ionic channels expressed as trimers and showing various functions. A subtype, the P2X4 receptor present on microglial cells is highly involved in neuropathic pain. In this study, in order to prepare antibodies recognizing the native structure of rat P2X4 (rP2X4) receptor, we immunized mice with rP2X4's head domain (rHD, Gln111-Val167), which possesses an intact structure stabilized by S-S bond formation (Igawa and Abe et al. FEBS Lett. 2015), as an antigen. We generated five monoclonal antibodies with the ability to recognize the native structure of its head domain, stabilized by S-S bond formation. Site-directed mutagenesis revealed that Asn127 and Asp131 of the rHD, in which combination of these amino acid residues is only conserved in P2X4 receptor among P2X family, were closely involved in the interaction between rHD and these antibodies. We also demonstrated the antibodies obtained here could detect rP2X4 receptor expressed in 1321N1 human astrocytoma cells..
3. Yoshito Abe, Naoki Odawara, Nantanat Aeimhirunkailas, Hinako Shibata, Naoki Fujisaki, Hirofumi Tachibana, Tadashi Ueda, Inhibition of amyloid fibril formation in the variable domain of λ6 light chain mutant Wil caused by the interaction between its unfolded state and epigallocatechin-3-O-gallate, Biochimica et Biophysica Acta - General Subjects, 10.1016/j.bbagen.2018.08.006, 1862, 12, 2570-2578, 2018.12.
4. Yoshito Abe, Seijiro Shioi, Shunsuke Kita, Hikaru Nakata, Katsumi Maenaka, Daisuke Kohda, Tsutomu Katayama, Tadashi Ueda, X‐ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation., FEBS letter, 592, 22, 3805-3816, 2017.10.
5. Yoshito Abe, Mitsuru Kubota, Shinya Takazaki, Yuji Ito, Hiromi Yamamoto, Kang Dongchon, Tadashi Ueda, Taiji Imoto, Effect on catalysis by replacement of catalytic residue from hen egg white lysozyme to Venerupis philippinarum lysozyme, Protein Science, 10.1002/pro.2966, 25, 9, 1637-1647, 2016.06.
6. Tatsuhiro Igawa, Yoshito Abe, Tsuda Makoto, Kazuhiko Inoue, Tadashi Ueda, Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding., FEBS letter, 589, 6, 680-686, 2015.03.
7. Saki Fujiyama, Yoshito Abe, Junya Tani, Masahi Urabe, Kenji Sato, Takahiko Aramaki, Tsutomu Katayama, Tadashi Ueda, Structure and mechanism of the primosome protein DnaT: functional structures for homotrimerization, dissociation of ssDNA from PriB-ssDNA complex and formation of DnaT-ssDNA complex, FEBS journal, 10.1111/febs.13080., 281, 23, 5356-5370, 2014.09.
8. Saki Fujiyama, Yoshito Abe, Taichi Takenawa, Takahiko Aramaki, Seijiro Shioi, Tsutomu Katayama, Tadashi Ueda, Involvement of histidine in complex formation of PriB and single-stranded DNA. , BBA proteins and proteomics, 1844, 2, 299-307, 2014.02.
9. Takahiko Aramaki, Yoshito Abe, Tsutomu Katayama, Tadashi Ueda, Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli., Protein Science, 10.1002/pro.2314, 22, 9, 1279-1286, 2013.07.
10. Takahiko Aramaki, Yoshito Abe, Takatoshi Ohkuri, Tomonori Mishima, Shoji Yamashita, Tsutomu Katayama, Tadashi Ueda, Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli. , Genes to Cells, 10.1111/gtc.12069, 18, 9, 723-732, 2013.07.
11. Masahiro Abe, Yoshito Abe, Takatoshi Ohkuri, mishima tomonori, 門司 晃, Shigenobu Kanba, Tadashi Ueda, Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein., Protein Science, 22, 4, 467-474, 2013.02.
12. Takazaki S, Abe Y, Yamaguchi T, Yagi M, Ueda T, Kang D, Hamasaki N, Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding, BBA – Biomembranes , 1818, 3, 658-65, Epub 2011 Dec 1, 2012.03.
13. Takazaki S, Abe Y, Yamaguchi T, Yagi M, Ueda T, Kang D, Hamasaki N, Mutation of His 834 in human anion exchanger 1 affects substrate binding, BBA – Biomembranes , 1798, 5, 903-908, 2010.03.
14. Goto T,Abe Y, Kakuta Y, Takeshita K, Imoto T, and Ueda T, Crystal structure of Tapes japonica lysozyme with substrate analogue ; Structural basis of the catalytic mechanism and manifestation of its chitinase activity accompany with quaternary structural change, J. Biol. Chem., 282; 27459-67, 2007.10.
15. Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T and Ueda T, Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC, J Biol Chem, 282: 17517-17529, 2007.07.
16. Li C, Takazaki S, Jin X, Kang D, Abe Y and Hamasaki N, Identification of Oxidized Methionine Sites in Erythrocyte Membrane Protein using LC/ESI MS Peptide Mapping, Biochemistry, 45(39), 12117 -12124, 2006.10.
17. Jin X, Abe Y, Li C, and Hamasaki N, Histidine-834 of Human Erythrocyte Band 3 has an essential role in the Conformational Changes that occur during the Band 3-mediated Anion Exchange, Biochemistry, 10.1021/bi0350809, 42, 44, 12927-12932, 42: 12927-12932, 2003.11.
18. Abe Y, Shodai T, Muto T, Mihara K, Torii H, Nishikawa S, Endo T, Kohda D, Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20, Cell, 10.1016/S0092-8674(00)80691-1, 100, 5, 551-560, 100:551-560, 2000.03.
19. Abe Y, Odaka M, Inagaki F, Lax I, Schlessinger J, Kohda D, Disulfide bond structure of human epidermal growth factor receptor, Journal of Biological Chemistry, 273:11150-11157, 1998.05.
1. 阿部 義人, Mechanism for Retardation of Amyloid Fibril Formation by Small Molecules in Vλ6 Protein
, The 2nd HU-TMU-KU Joint Symposium for Pharmaceutical Sciences, 2016.09.
2. Yoshito Abe, Saki Fujiyama, Takahiko Aramaki, Tsutome Katayama, Tadashi Ueda, Structure and mechanism of the replication restart primosome proteins, 日本生化学会, 2014.10.
3. Structure and Function of human erythrocyte band 3
Yoshito Abe, Naotaka Hamasaki.
Educational Activities
the lecture for graduate students; protein science
the lecture for undergraduate; protein science, immunology, biochemistry
Other Educational Activities
  • 2015.07.
  • 2014.07.