Claim · model-written summary
OsMlo binds soybean SCaM-1 in a calcium-dependent manner.
- Taxon
- rice
Oryza sativat0 - Gene
- OsMloe0
- Outcome
- binds to soybean CaM isoform-1 (SCaM-1)e0
- Qualifier
- in a Ca(2+)-dependent mannere0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“OsMlo produced in Escherichia coli binds to soybean CaM isoform-1 (SCaM-1) in a Ca(2+)-dependent manner”
t0“rice Mlo (Oryza sativa Mlo; OsMlo)”
Title
Mlo, a Modulator of Plant Defense and Cell Death, Is a Novel Calmodulin-binding Protein
Min Chul Kim; Sang Hyoung Lee; Jong Kyong Kim; et al. Journal of Biological Chemistry 2002. doi:10.1074/jbc.m108478200
Other claims from this paper (8)
- Observation A rice Mlo gene was isolated from pathogen-elicited rice cells.
- Observation OsMlo has a molecular mass of 62 kDa.
- Observation OsMlo shares 65% sequence identity and scaffold topology with barley Mlo.
- Mechanism A 20-amino acid domain in the OsMlo C-terminal tail is necessary and sufficient for calcium-dependent calmodulin complex formation.
- Observation Conserved CaMBD binding to CaM was corroborated by three assays.
- Intervention effect A fungal pathogen strongly induced OsMlo expression.
- Intervention effect Plant defense signaling molecules strongly induced OsMlo expression.
- Mechanism Authors propose that calcium-loaded CaM binding to the C-terminal tail may be common among Mlo proteins.