start-ver=1.4
cd-journal=joma
no-vol=8
cd-vols=
no-issue=6
article-no=
start-page=923
end-page=938
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2006
dt-pub=20066
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=A glycosylation island is a genetic region required for glycosylation. The glycosylation island of flagellin in Pseudomonas syringae pv. tabaci 6605 consists of three orfs: orf1, orf2 and orf3. Orf1 and orf2 encode putative glycosyltransferases, and their deletion mutants, Delta orf1 and Delta orf2, exhibit deficient flagellin glycosylation or produce partially glycosylated flagellin respectively. Digestion of glycosylated flagellin from wild-type bacteria and non-glycosylated flagellin from Delta orf1 mutant using aspartic N-peptidase and subsequent HPLC analysis revealed candidate glycosylated amino acids. By generation of site-directed Ser/Ala-substituted mutants, all glycosylated amino acid residues were identified at positions 143, 164, 176, 183, 193 and 201. Matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry (MS) analysis revealed that each glycan was about 540 Da. While all glycosylation-defective mutants retained swimming ability, swarming ability was reduced in the Delta orf1, Delta orf2 and Ser/Ala-substituted mutants. All glycosylation mutants were also found to be impaired in the ability to adhere to a polystyrene surface and in the ability to cause disease in tobacco. Based on the predicted tertiary structure of flagellin, S176 and S183 are expected to be located on most external surface of the flagellum. Thus the effect of Ala-substitution of these serines is stronger than that of other serines. These results suggest that glycosylation of flagellin in P. syringae pv. tabaci 6605 is required for bacterial virulence. It is also possible that glycosylation of flagellin may mask elicitor function of flagellin molecule.
en-copyright=
kn-copyright=

en-aut-name=TaguchiFumiko
en-aut-sei=Taguchi
en-aut-mei=Fumiko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=TakeuchiKasumi
en-aut-sei=Takeuchi
en-aut-mei=Kasumi
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aut-affil-num=2
ORCID=

en-aut-name=KatohEtsuko
en-aut-sei=Katoh
en-aut-mei=Etsuko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=MurataKatsuyoshi
en-aut-sei=Murata
en-aut-mei=Katsuyoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=SuzukiTomoko
en-aut-sei=Suzuki
en-aut-mei=Tomoko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

en-aut-name=MarutaniMizuri
en-aut-sei=Marutani
en-aut-mei=Mizuri
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=6
ORCID=

en-aut-name=KawasakiTakayuki
en-aut-sei=Kawasaki
en-aut-mei=Takayuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=7
ORCID=

en-aut-name=EguchiMinako
en-aut-sei=Eguchi
en-aut-mei=Minako
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=8
ORCID=

en-aut-name=KatohShizue
en-aut-sei=Katoh
en-aut-mei=Shizue
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=9
ORCID=

en-aut-name=kakuHanae
en-aut-sei=kaku
en-aut-mei=Hanae
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=10
ORCID=

en-aut-name=YasudaChihiro
en-aut-sei=Yasuda
en-aut-mei=Chihiro
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=11
ORCID=

en-aut-name=InagakiYoshishige
en-aut-sei=Inagaki
en-aut-mei=Yoshishige
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=12
ORCID=

en-aut-name=ToyodaKazuhiro
en-aut-sei=Toyoda
en-aut-mei=Kazuhiro
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=13
ORCID=

en-aut-name=ShiraishiTomonori
en-aut-sei=Shiraishi
en-aut-mei=Tomonori
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=14
ORCID=

en-aut-name=IchinoseYuki
en-aut-sei=Ichinose
en-aut-mei=Yuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=15
ORCID=

affil-num=1
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=2
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=3
en-affil=
kn-affil=National Institute of Agrobiological Sciences

affil-num=4
en-affil=
kn-affil=National Institute of Agrobiological Sciences

affil-num=5
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=6
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=7
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=8
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=9
en-affil=
kn-affil=National Institute of Agrobiological Sciences

affil-num=10
en-affil=
kn-affil=National Institute of Agrobiological Sciences

affil-num=11
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=12
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=13
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=14
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University

affil-num=15
en-affil=
kn-affil=The Graduate School of Natural Science and Technology, Okayama University
en-keyword=Gram-Negative bacteria
kn-keyword=Gram-Negative bacteria
en-keyword=Posttranslational modification
kn-keyword=Posttranslational modification
en-keyword=Protein Glycosylation
kn-keyword=Protein Glycosylation
en-keyword=Perception
kn-keyword=Perception
en-keyword=Aeruginosa
kn-keyword=Aeruginosa
en-keyword=Cells
kn-keyword=Cells
en-keyword=Specificity
kn-keyword=Specificity
en-keyword=Expression
kn-keyword=Expression
en-keyword=Plasmids
kn-keyword=Plasmids
en-keyword=Pathways
kn-keyword=Pathways
END

start-ver=1.4
cd-journal=joma
no-vol=63
cd-vols=
no-issue=1
article-no=
start-page=o17
end-page=o20
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2007
dt-pub=200701
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Hydrogen bonding in two solid phases of phenazine-chloranilic acid (1/1) determined at 170 and 93 K
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=The crystal structures in two solid phases, i.e. phase II stable between 146 and 253 K and phase IV below 136 K, of the title compound [phenazine-chloranilic acid (1/1), C12H8N2 center dot C6H2Cl2O4, in phase II, and phenazinium hydrogen chloranilate, C12H9N2+center dot C6HCl2O4-, in phase IV], have been determined. Both phases crystallize in P2(1), and each structure was refined as an inversion twin. In phase II, the phenazine and chloranilic acid molecules are arranged alternately through two kinds of O-H center dot center dot center dot N hydrogen bonds. In phase IV, salt formation occurs by donation of one H atom from the chloranilic acid molecule to the phenazine molecule; the resulting monocation and monoanion are linked by N-H center dot center dot center dot O and O-H center dot center dot center dot N hydrogen bonds.
en-copyright=
kn-copyright=

en-aut-name=GotohKazuma
en-aut-sei=Gotoh
en-aut-mei=Kazuma
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=AsajiTetsuo
en-aut-sei=Asaji
en-aut-mei=Tetsuo
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=IshidaHiroyuki
en-aut-sei=Ishida
en-aut-mei=Hiroyuki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Chemistry, Faculty of Science, Okayama University

affil-num=2
en-affil=
kn-affil=Department of Chemistry, Graduate School of Integrated Basic Sciences, College of Humanities and Sciences, Nihon University

affil-num=3
en-affil=
kn-affil=Department of Chemistry, Faculty of Science, Okayama University
END