BROWSE

Related Researcher

Author

Cho, Moo Je
Ulsan National Institute of Science and Technology
Research Interests
  • Calcium Signaling

ITEM VIEW & DOWNLOAD

Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein - Isolation and characterization of a rice Mlo homologue

Cited 60 times inthomson ciCited 60 times inthomson ci
Title
Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein - Isolation and characterization of a rice Mlo homologue
Author
Kim, MCLee, SHKim, JKChun, HJChoi, MSChung, WSMoon, BCKang, CHPark, Chan YoungYoo, JHKang, YHKoo, SCKoo, YDJung, JCKim, STSchulze-Lefert, PLee, SYCho, Moo Je
Keywords
HYPERSENSITIVE DISEASE RESISTANCE; NITRIC-OXIDE SYNTHASE; LIGHT-CHAIN KINASE; OXIDATIVE BURST; FUNGAL ELICITOR; POWDERY MILDEW; GLUTAMATE-DECARBOXYLASE; CYTOSOLIC CALCIUM; PLASMA-MEMBRANE; PEPTIDE COMPLEX
Issue Date
200205
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.22, pp.19304 - 19314
Abstract
Transient influx of Ca2+ constitutes an early event in the signaling cascades that trigger plant defense responses. However, the downstream components of defense-associated Ca2+ signaling are largely unknown. Because Ca2+ signals are mediated by Ca2+-binding proteins, including calmodulin (CaM), identification and characterization of CaM-binding proteins elicited by pathogens should provide insights into the mechanism by which Ca2+ regulates defense responses. In this study, we isolated a gene encoding rice Mlo (Oryza sativa Mlo; OsMlo) using a protein-protein interaction-based screening of a cDNA expression library constructed from pathogen-elicited rice suspension cells. OsMlo has a molecular mass of 62 kDa and shares 65% sequence identity and scaffold topology with barley Mlo, a heptahelical transmembrane protein known to function as a negative regulator of broad spectrum disease resistance and leaf cell death. By using gel overlay assays, we showed that OsMlo produced in Escherichia coli binds to soybean CaM isoform-1 (SCaM-1) in a Ca2+-dependent manner. We located a 20-amino acid CaM-binding domain (CaMBD) in the OsMlo C-terminal cytoplasmic tail that is necessary and sufficient for Ca2+-dependent CaM complex formation. Specific binding of the conserved CaMBD to CaM was corroborated by site-directed mutagenesis, a gel mobility shift assay, and a competition assay with a Ca2+/CaM-dependent enzyme. Expression of OsMlo was strongly induced by a fungal pathogen and by plant defense signaling molecules. We propose that binding of Ca2+-loaded CaM to the C-terminal tail may be a common feature of Mlo proteins.
URI
Go to Link
DOI
http://dx.doi.org/10.1074/jbc.M108478200
ISSN
0021-9258
Appears in Collections:
SLS_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qr_code

  • mendeley

    citeulike

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

MENU