File Download

There are no files associated with this item.

  • Find it @ UNIST can give you direct access to the published full text of this article. (UNISTARs only)
Related Researcher

조무제

Cho, Moo Je
Read More

Views & Downloads

Detailed Information

Cited time in webofscience Cited time in scopus
Metadata Downloads

Full metadata record

DC Field Value Language
dc.citation.endPage 534 -
dc.citation.number 3 -
dc.citation.startPage 523 -
dc.citation.title PLANT MOLECULAR BIOLOGY -
dc.citation.volume 37 -
dc.contributor.author Kim, CY -
dc.contributor.author Gal, SW -
dc.contributor.author Choe, MS -
dc.contributor.author Jeong, SY -
dc.contributor.author Lee, SI -
dc.contributor.author Cheong, YH -
dc.contributor.author Lee, SH -
dc.contributor.author Choi, YJ -
dc.contributor.author Han, CD -
dc.contributor.author Kang, KY -
dc.contributor.author Cho, Moo Je -
dc.date.accessioned 2023-12-22T12:36:07Z -
dc.date.available 2023-12-22T12:36:07Z -
dc.date.created 2014-09-22 -
dc.date.issued 1998-06 -
dc.description.abstract Among the four classes of chitinase, a class II chitinase had not yet been reported for rice. We have isolated and characterized a class II acidic chitinase, Rcht2, from rice (Oryza sativa L. cv. Cheongcheongbyeo). The protein consists of a single polypeptide chain of 261 amino acid residues and includes a putative signal sequence of 29 amino acids at its N-terminus. It has a calculated molecular mass of 27 642 Da and an isoelectric point of 5.56. The Rcht2 chitinase lacks the cysteine-rich and hinge domains in the N-terminal region of the protein, which is the criterion for its classification as a class II chitinase. Comparison of the genomic and the cDNA sequence revealed that the coding region of Rcht2 consist of three exons of 301, 112, and 370 bp separated by two introns of 89 and 984 bp. In suspension-cultured rice cells, the transcript level of Rcht2 was dramatically increased by treatment with both glycol chitin and fungal elicitor. The application of protein phosphatase 1 and 2A inhibitors, calyculin A and okadaic acid, effectively abolished the induction of Rcht2 in response to fungal elicitor. In contrast, the activation of Rcht2 transcript was not inhibited by both cycloheximide and protein kinase inhibitors. These results demonstrate that protein dephosphorylation events play a crucial role in the elicitor-mediated induction of Rcht2 in rice cells, while de novo protein synthesis is not required for induction. -
dc.identifier.bibliographicCitation PLANT MOLECULAR BIOLOGY, v.37, no.3, pp.523 - 534 -
dc.identifier.doi 10.1023/A:1005960313459 -
dc.identifier.issn 0167-4412 -
dc.identifier.scopusid 2-s2.0-2142773623 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/6368 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=2142773623 -
dc.identifier.wosid 000073678800010 -
dc.language 영어 -
dc.publisher SPRINGER -
dc.title A new class II rice chitinase, Rcht2, whose induction by fungal elicitor is abolished by protein phosphatase 1 and 2A inhibitor -
dc.type Article -
dc.description.journalRegisteredClass scopus -

qrcode

Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.