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ID 32975
フルテキストURL
著者
Taguchi, Fumiko The Graduate School of Natural Science and Technology, Okayama University
Takeuchi, Kasumi The Graduate School of Natural Science and Technology, Okayama University
Katoh, Etsuko National Institute of Agrobiological Sciences
Murata, Katsuyoshi National Institute of Agrobiological Sciences
Suzuki, Tomoko The Graduate School of Natural Science and Technology, Okayama University
Marutani, Mizuri The Graduate School of Natural Science and Technology, Okayama University
Kawasaki, Takayuki The Graduate School of Natural Science and Technology, Okayama University
Eguchi, Minako The Graduate School of Natural Science and Technology, Okayama University
Katoh, Shizue National Institute of Agrobiological Sciences
kaku, Hanae National Institute of Agrobiological Sciences
Yasuda, Chihiro The Graduate School of Natural Science and Technology, Okayama University
Inagaki, Yoshishige The Graduate School of Natural Science and Technology, Okayama University
Toyoda, Kazuhiro The Graduate School of Natural Science and Technology, Okayama University
Shiraishi, Tomonori The Graduate School of Natural Science and Technology, Okayama University
Ichinose, Yuki The Graduate School of Natural Science and Technology, Okayama University
抄録
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.
キーワード
Gram-Negative bacteria
Posttranslational modification
Protein Glycosylation
Perception
Aeruginosa
Cells
Specificity
Expression
Plasmids
Pathways
備考
Digital Object Identifer:10.1111/j.1462-5822.2005.00674.x
Published with permission from the copyright holder. This is the author's copy, as published in Cellular Microbiology, June 2006, Volume 8, Issue 6, Pages 923-938. Publisher URL:http://dx.doi.org/10.1111/j.1462-5822.2005.00674.x
Direct access to Thomson Web of Science record
Copyright © 2006 The Authors Journal compilation © 2006 Blackwell Publishing Ltd.
発行日
2006-6
出版物タイトル
Cellular Microbiology
8巻
6号
出版者
Blackwell Publishing
開始ページ
923
終了ページ
938
ISSN
1462-5814
NCID
AA1136678X
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
著作権者
The Authors, Journal compilation : Blackwell Publishing Ltd
論文のバージョン
author
査読
有り
DOI
PubMed ID
Web of Sience KeyUT
Submission Path
biology_general/24