Skip Navigation


Glycobiology Advance Access originally published online on February 29, 2008
Glycobiology 2008 18(5):414-423; doi:10.1093/glycob/cwn018
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Supplementary Data
Right arrow All Versions of this Article:
18/5/414    most recent
cwn018v2
cwn018v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (2)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Onaga, S.
Right arrow Articles by Taira, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Onaga, S.
Right arrow Articles by Taira, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

A new type of plant chitinase containing LysM domains from a fern (Pteris ryukyuensis): Roles of LysM domains in chitin binding and antifungal activity

Shoko Onaga and Toki Taira1

Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyu University, Okinawa 903-0213, Japan

1 To whom correspondence should be addressed: Tel: +81-98-895-8802; Fax: +81-98-895-8802; e-mail: tokey{at}agr.u-ryukyu.ac.jp

Received on October 26, 2007; revised on February 19, 2008; accepted on February 20, 2008

Chitinase-A (PrChi-A), of molecular mass 42 kDa, was purified from the leaves of a fern (P. ryukyuensis) using several column chromatographies. The N-terminal amino acid sequence of PrChi-A was similar to the lysin motif (LysM). A cDNA encoding PrChi-A was cloned by rapid amplification of cDNA ends and polymerase chain reaction. It consisted of 1459 nucleotides and encoded an open-reading frame of 423-amino-acid residues. The deduced amino acid sequence indicated that PrChi-A is composed of two N-terminal LysM domains and a C-terminal catalytic domain, belonging to the group of plant class IIIb chitinases, linked by proline, serine, and threonine-rich regions. Wild-type PrChi-A had chitin-binding and antifungal activities, but a mutant without LysM domains had lost both activities. These results suggest that the LysM domains contribute significantly to the antifungal activity of PrChi-A through their binding activity to chitin in the cell wall of fungi. This is the first report of the presence in plants of a family-18 chitinase containing LysM domains.

Key words: antifungal activity / chitin binding / family 18 chitinase / LysM/plant chitinase


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
S. Shridhar, D. Chattopadhyay, and G. Yadav
PLecDom: a program for identification and analysis of plant lectin domains
Nucleic Acids Res., July 1, 2009; 37(suppl_2): W452 - W458.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
D. J. Rigden and M. Y. Galperin
Sequence analysis of GerM and SpoVS, uncharacterized bacterial 'sporulation' proteins with widespread phylogenetic distribution
Bioinformatics, August 15, 2008; 24(16): 1793 - 1797.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.