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Title 

CHRK1, a chitinase-related receptor-like kinase in tobacco

Authors 

Youn Sung KimJeong Hee LeeGyeong Mee YoonHye Sun ChoSeong Whan ParkMi Chung SuhDo Il ChoiHyun Jung HaJang Ryol LiuHyun Sook Pai

Publisher 

American Society of Plant Biologists

Issue Date 

2000

Citation 

Plant Physiology, vol. 123, no. 3, pp. 905-915

Keywords 

amino acid sequencecarboxy terminal sequencechitinase related receptor like kinasechitinaseCHRK1complementary DNAenzyme activityfungal infectionglutamic acidmessenger RNA

Abstract 

A cDNA encoding a chitinase-related receptor-like kinase, designated CHRK1, was isolated from tobacco(Nicotiana tabacum). The C-terminal kinase domain (KD) of CHRK1 contained all of the conserved amino acids of serine/threonine protein kinases. The putative extracellular domain was closely related to the class V chitinase of tobacco and to microbial chitinases. CHRK1 mRNA accumulation was strongly stimulated by infection with fungal pathogen and tobacco mosaic virus. Amino acid-sequence analysis revealed that the chitinase-like domain of CHRK1 lacked the essential glutamic acid residue required for chitinase activity. The recombinant chitinase-like domain did not show any catalytic activity for either oligomeric or polymeric chitin substrates. The recombinant KD of CHRK1 exhibited autophosphorylation, but the mutant KD with a mutation in the essential ATP-binding site did not, suggesting that CHRK1 encoded a functional kinase. CHRK1 was detected in membrane fractions of tobacco BY2 cells. Furthermore, CHRKI-GFP fusion protein was localized in plasma membranes when it was expressed in animal cells. This is the first report of a new type of receptor-like kinase containing a chitinase-like sequence in the putative extracellular domain.

ISSN 

0032-0889

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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