Tasuku Hamaguchi
Osaka City University
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Tasuku Hamaguchi.
Glycobiology | 2010
Tasuku Hamaguchi; Tsukasa Ito; Yukako Inoue; Tipaporn Limpaseni; Piamsook Pongsawasdi; Kazuo Ito
Endo-beta-N-acetylglucosaminidases are thought to be key enzymes in the catabolism of asparagine-linked oligosaccharides. However, little is known about the enzymes of this type in basidiomycetes. We investigated endo-beta-N-acetylglucosaminidases in basidiomycetes using fluorescence-labeled glycoasparagines as substrates. Flammulina velutipes showed high activity and its enzyme was named endo-beta-N-acetylglucosaminidase FV (Endo FV). The enzyme purified from the fruiting bodies of F. velutipes was separated into two forms. Endo FV was specific for high mannose and hybrid-type oligosaccharides. The enzyme was remarkably less active against asparagine-linked oligosaccharides attached to glycoproteins. It transferred an asparagine-linked oligosaccharide to Glc, but not to Gal. cDNA of Endo FV was cloned. It was composed of a 996-bp open reading frame encoding 331 amino acid residues. A recombinant Endo FV expressed in Escherichia coli showed enzymatic activity. The Endo FV gene in the genome of F. velutipes had no introns. The gene encoding Endo FV showed little homology with genes of known endo-beta-N-acetylglucosaminidases. A chitinase active site motif existed in the deduced primary structure, indicating that Endo FV belongs to glycoside hydrolase family 18. The deduced amino acid sequence of Endo FV had regions conserved in class III chitinases from fungi though it showed little homology with the sequence of any other endo-beta-N-acetylglucosaminidases. A folding model of Endo FV indicated it to be homologous with the tertiary structure of Endo H which is quite similar in specificity for asparagine-linked oligosaccharides. This study suggests that Endo FV may become similar to Endo H in substrate specificity as a result of evolutionary convergence.
Current Opinion in Microbiology | 2016
Makoto Miyata; Tasuku Hamaguchi
Mycoplasma mobile forms gliding machinery at a cell pole and glides continuously in the direction of the cell pole at up to 4.5μm per second on solid surfaces such as animal cells. This motility system is not related to those of any other bacteria or eukaryotes. M. mobile uses ATP energy to repeatedly catch, pull, and release sialylated oligosaccharides on host cells with its approximately 50-nm long legs. The gliding machinery is a large structure composed of huge surface proteins and internal jellyfish-like structure. This system may have developed from an accidental combination between an adhesin and a rotary ATPase, both of which are essential for the adhesive parasitic life of Mycoplasmas.
Frontiers in Microbiology | 2016
Makoto Miyata; Tasuku Hamaguchi
Mycoplasma pneumoniae forms a membrane protrusion at a cell pole and is known to adhere to solid surfaces, including animal cells, and can glide on these surfaces with a speed up to 1 μm per second. Notably, gliding appears to be involved in the infectious process in addition to providing the bacteria with a means of escaping the hosts immune systems. However, the genome of M. pneumoniae does not encode any of the known genes found in other bacterial motility systems or any conventional motor proteins that are responsible for eukaryotic motility. Thus, further analysis of the mechanism underlying M. pneumoniae gliding is warranted. The gliding machinery formed as the membrane protrusion can be divided into the surface and internal structures. On the surface, P1 adhesin, a 170 kDa transmembrane protein forms an adhesin complex with other two proteins. The internal structure features a terminal button, paired plates, and a bowl (wheel) complex. In total, the organelle is composed of more than 15 proteins. By integrating the currently available information by genetics, microscopy, and structural analyses, we have suggested a working model for the architecture of the organelle. Furthermore, in this article, we suggest and discuss a possible mechanism of gliding based on the structural model, in which the force generated around the bowl complex transmits through the paired plates, reaching the adhesin complex, resulting in the repeated catch of sialylated oligosaccharides on the host surface by the adhesin complex.
Journal of Bacteriology | 2015
Taishi Kasai; Tasuku Hamaguchi; Makoto Miyata
UNLABELLED The binding and gliding of Mycoplasma mobile on a plastic plate covered by 53 uniform oligosaccharides were analyzed. Mycoplasmas bound to and glided on only 21 of the fixed sialylated oligosaccharides (SOs), showing that sialic acid is essential as the binding target. The affinities were mostly consistent with our previous results on the inhibitory effects of free SOs and suggested that M. mobile recognizes SOs from the nonreducing end with four continuous sites as follows. (i and ii) A sialic acid at the nonreducing end is tightly recognized by tandemly connected two sites. (iii) The third site is recognized by a loose groove that may be affected by branches. (iv) The fourth site is recognized by a large groove that may be enhanced by branches, especially those with a negative charge. The cells glided on uniform SOs in manners apparently similar to those of the gliding on mixed SOs. The gliding speed was related inversely to the mycoplasmas affinity for SO, suggesting that the detaching step may be one of the speed determinants. The cells glided faster and with smaller fluctuations on the uniform SOs than on the mixtures, suggesting that the drag caused by the variation in SOs influences gliding behaviors. IMPORTANCE Mycoplasma is a group of bacteria generally parasitic to animals and plants. Some Mycoplasma species form a protrusion at a pole, bind to solid surfaces, and glide in the direction of the protrusion. These procedures are essential for parasitism. Usually, mycoplasmas glide on mixed sialylated oligosaccharides (SOs) derived from glycoprotein and glycolipid. Since gliding motility on uniform oligosaccharides has never been observed, this study gives critical information about recognition and interaction between receptors and SOs.
Archives of Biochemistry and Biophysics | 2006
Kazuo Ito; Kimiko Miyagawa; Mutsumi Matsumoto; Shigeki Yabuno; Naoko Kawakami; Tasuku Hamaguchi; Masaru Iizuka; Noshi Minamiura
Journal of applied glycoscience | 2007
Kimiko Miyagawa; Mutsumi Matsumoto; Shigeki Yabuno; Naoko Kawakami; Tasuku Hamaguchi; Masaru Iizuka; Noshi Minamiura; Kazuo Ito
Seibutsu Butsuri | 2017
Tasuku Hamaguchi; Masaru Kawakami; Makoto Miyata
Journal of Electron Microscopy | 2015
U Matsumoto; Yoshito Kawakita; Tsuyoshi Kenri; Shigetaro Mori; Tasuku Hamaguchi; Miki Kinoshita; Akihiro Kawamoto; Takayuki Kato; Keiichi Namba; Makoto Miyata
Journal of Electron Microscopy | 2015
Daiki Matsuike; Yuhei Tahara; Tasuku Hamaguchi; Makoto Miyata
Current Opinion in Microbiology | 2015
Makoto Miyata; Tasuku Hamaguchi