Faculty Profiles - HAYASHI Gosuke

Papers - HAYASHI Gosuke

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Hybridization-sensitive Fluorescent Oligonucleotide Probe Conjugated with Cell-penetrating Peptides for Enhanced Cellular Uptake

Hayashi Gosuke, Tamai Makoto, Okamoto Akimitsu

CHEMISTRY LETTERS Vol. 46 ( 12 ) page： 1803-1806 - 1806 2017.12

Language：English Publishing type：Research paper (scientific journal) Publisher：The Chemical Society of Japan

<p>Intracellular delivery of oligonucleotides is essential not only for antisense- and RNAi-therapeutics, but also for live-cell RNA imaging with fluorescent nucleic acid probes. Herein, we developed oligonucleotide–peptide conjugates synthesized via Cu-catalyzed alkyne-azide cycloaddition between an exciton-controlled hybridization-sensitive oligonucleotide (ECHO) probe and linear or cyclic cell-penetrating peptides (CPPs). When lipofected to living HeLa cells, the CPP-conjugated ECHO probe showed enhanced cellular uptake efficiency compared with that of the unconjugated ECHO probe.</p>

DOI： 10.1246/cl.170813

Regulation of the Stability of the Histone H2A-H2B Dimer by H2A Tyr57 Phosphorylation.

Sueoka T, Hayashi G, Okamoto A

Biochemistry Vol. 56 ( 36 ) page： 4767-4772 - 4772 2017.9

Chemical synthesis of dual labeled proteins via differently protected alkynes enables intramolecular FRET analysis.

Hayashi G, Kamo N, Okamoto A

Chemical communications (Cambridge, England) Vol. 53 ( 43 ) page： 5918-5921 - 5921 2017.5

Chemically-activatable alkyne-tagged probe for imaging microdomains in lipid bilayer membranes.

Yamaguchi S, Matsushita T, Izuta S, Katada S, Ura M, Ikeda T, Hayashi G, Suzuki Y, Kobayashi K, Tokunaga K, Ozeki Y, Okamoto A

Scientific reports Vol. 7 page： 41007 2017.1

Base-Resolution Analysis of 5-Hydroxymethylcytosine by One-Pot Bisulfite-Free Chemical Conversion with Peroxotungstate.

Hayashi G, Koyama K, Shiota H, Kamio A, Umeda T, Nagae G, Aburatani H, Okamoto A

Journal of the American Chemical Society Vol. 138 ( 43 ) page： 14178-14181 - 14181 2016.11

In vitro and in cell analysis of chemically synthesized histone H2A with multiple modifications.

Hayashi G, Sueoka T, Okamoto A

Chemical communications (Cambridge, England) Vol. 52 ( 28 ) page： 4999-5002 - 5002 2016.4

Diazirine Photocrosslinking Recruits Activated FTO Demethylase Complexes for Specific N-6-methyladenosine Recognition Reviewed

Hyun Seok Jeong, Gosuke Hayashi, Akimitsu Okamoto

ACS CHEMICAL BIOLOGY Vol. 10 ( 6 ) page： 1450 - 1455 2015.6

Language：English Publishing type：Research paper (scientific journal) Publisher：AMER CHEMICAL SOC

N-6-methyladenosine (m(6)A) is a prevalent modification of RNAs. m(6)A exists in mRNA and plays an important role in RNA biological pathways and in RNA epigenetic regulation, We applied diazirine photocrosslinking to the event of m(6)A recognition mediated by the fat mass and obesity associated (FTO) demethylase. A highly photoreactive diazirine adjacent to m(6)A on the RNA successfully recruited activated FTO complexes with an m(6)A preference. The process of recognition of m(6)A via FTO using diazirine photocrosslinking was controlled by the alpha-ketoglutarate (alpha-KG) cosubstrate and the Peal). cofactor, which are involved in m(6)A oxidative demethylation. In addition, FTO bound to ssRNAs prior to the m(6)A recognition process. Diazirine photocrosslinking contributes to increasing the chances of capturing activated FTO complexes with specific m(6)A recognition and provides new insights into the dynamic FTO oxidative demethylation process.

DOI： 10.1021/cb5010096

Web of Science

PubMed

2-Oxazoline formation for selective chemical labeling of 5-hydroxylysine.

Hayashi G, Sakamoto R, Okamoto A

Chemistry, an Asian journal Vol. 10 ( 5 ) page： 1138-41 - 41 2015.5

Hybridization-sensitive fluorescent oligonucleotide probe conjugated with a bulky module for compartment-specific mRNA monitoring in a living cell.

Hayashi G, Yanase M, Takeda K, Sakakibara D, Sakamoto R, Wang DO, Okamoto A

Bioconjugate chemistry Vol. 26 ( 3 ) page： 412-7 - 7 2015.3

Middle-Down and Chemical Proteomic Approaches to Reveal Histone H4 Modification Dynamics in Cell Cycle: Label-Free Semi-Quantification of Histone Tail Peptide Modifications Including Phosphorylation and Highly Sensitive Capture of Histone PTM Binding Proteins Using Photo-Reactive Crosslinkers.

Yamamoto K, Chikaoka Y, Hayashi G, Sakamoto R, Yamamoto R, Sugiyama A, Kodama T, Okamoto A, Kawamura T

Mass spectrometry (Tokyo, Japan) Vol. 4 ( 1 ) page： A0039 - A0039 2015

Language：English Publishing type：Research paper (scientific journal) Publisher：The Mass Spectrometry Society of Japan

Mass spectrometric proteomics is an effective approach for identifying and quantifying histone post-translational modifications (PTMs) and their binding proteins, especially in the cases of methylation and acetylation. However, another vital PTM, phosphorylation, tends to be poorly quantified because it is easily lost and inefficiently ionized. In addition, PTM binding proteins for phosphorylation are sometimes resistant to identification because of their variable binding affinities. Here, we present our efforts to improve the sensitivity of detection of histone H4 tail peptide phosphorylated at serine 1 (H4S1ph) and our successful identification of an H4S1ph binder candidate by means of a chemical proteomics approach.Our nanoLC-MS/MS system permitted semi-quantitative label-free analysis of histone H4 PTM dynamics of cell cycle-synchronized HeLa S3 cells, including phosphorylation, methylation, and acetylation. We show that H4S1ph abundance on nascent histone H4 unmethylated at lysine 20 (H4K20me0) peaks from late S-phase to M-phase. We also attempted to characterize effects of phosphorylation at H4S1 on protein–protein interactions. Specially synthesized photoaffinity bait peptides specifically captured 14-3-3 proteins as novel H4S1ph binding partners, whose interaction was otherwise undetectable by conventional peptide pull-down experiments.This is the first report that analyzes dynamics of PTM pattern on the whole histone H4 tail during cell cycle and enables the identification of PTM binders with low affinities using high-resolution mass spectrometry and photo-affinity bait peptides.

DOI： 10.5702/massspectrometry.A0039

PubMed

An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center.

Terasaka N, Hayashi G, Katoh T, Suga H

Nature chemical biology Vol. 10 ( 7 ) page： 555-7 - 557 2014.7

Development of photoswitchable RNA aptamer-ligand complexes.

Hayashi G, Nakatani K

Methods in molecular biology (Clifton, N.J.) Vol. 1111 page： 29-40 - 40 2014

Probe design for the effective fluorescence imaging of intracellular RNA.

Hayashi G, Okamoto A

Chemical record (New York, N.Y.) Vol. 13 ( 2 ) page： 209-17 - 17 2013.4

A nucleic acid probe labeled with desmethyl thiazole orange: a new type of hybridization-sensitive fluorescent oligonucleotide for live-cell RNA imaging.

Okamoto A, Sugizaki K, Yuki M, Yanagisawa H, Ikeda S, Sueoka T, Hayashi G, Wang DO

Organic & biomolecular chemistry Vol. 11 ( 2 ) page： 362-71 - 71 2013.1

Activation of prokaryotic translation by antisense oligonucleotides binding to coding region of mRNA.

Hayashi G, Hong C, Hagihara M, Nakatani K

Biochemical and biophysical research communications Vol. 429 ( 1-2 ) page： 105-10 - 10 2012.12

The RNA origin of transfer RNA aminoacylation and beyond.

Suga H, Hayashi G, Terasaka N

Philosophical transactions of the Royal Society of London. Series B, Biological sciences Vol. 366 ( 1580 ) page： 2959-64 - 64 2011.10

[Ribosomal synthesis of nonstandard cyclic peptides and its application to drug discovery].

Hayashi G, Ohshiro Y, Suga H

Seikagaku. The Journal of Japanese Biochemical Society Vol. 82 ( 6 ) page： 505-14 2010.6

[Ribosomal synthesis of nonstandard cyclic peptides and its application to drug discovery].

Hayashi G, Ohshiro Y, Suga H

Seikagaku. The Journal of Japanese Biochemical Society Vol. 82 ( 6 ) page： 505 - 14 2010.6

Ribosome evolution for two artificial amino acids in E. coli. International journal

Hayashi G, Goto Y, Suga H

Chemistry & biology Vol. 17 ( 4 ) page： 320-1 - 1 2010.4

RNA aptamers that reversibly bind photoresponsive azobenzene-containing peptides.

Hayashi G, Hagihara M, Nakatani K

Chemistry (Weinheim an der Bergstrasse, Germany) Vol. 15 ( 2 ) page： 424-32 - 32 2009

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Papers - HAYASHI Gosuke