Claim · model-written summary
Deletion mutagenesis mapped the chlorosis-inducing domain to amino acids 50 to 157 of the SPMV capsid protein.
- Taxon
- Panicum miliaceum
Panicum miliaceume1 - Interactor
- Satellite panicum mosaic virusPanicum mosaic satellite viruse0pathogen
- Gene
- SPMV CPe2
- Outcome
- chlorosis-inducing domaine2
- Value
- amino acids 50 to 157e2
Not reportedMaterialCompoundOrgan / stageSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e2“Initial deletion mutagenesis experiments mapped the chlorosis-inducing domain to amino acids 50 to 157 on the C-terminal portion of the SPMV CP”
e1“identifies additional biological activities of the SPMV CP, including the induction of severe chlorosis on proso millet plants (Panicum miliaceum cv. Sunup or Red Turghai)”
e0“Satellite panicum mosaic virus (SPMV), an 824-nucleotide, positive-sense, single-stranded RNA virus”
Title
Wenping Qiu; Karen-Beth G. Scholthof Molecular Plant-Microbe Interactions 2001. doi:10.1094/mpmi.2001.14.1.21
Other claims from this paper (6)
- Observation The SPMV capsid protein induced severe chlorosis on proso millet plants.
- Observation Amino acids 124 to 135 formed a critical domain for chlorosis induction and virion formation.
- Intervention effect Extreme C-terminal residues 148 to 157 were not strictly essential for chlorosis induction or virion formation.
- Intervention effect Absence of SPMV capsid protein tended to stimulate accumulation of defective RNAs.
- Mechanism The SPMV capsid protein likely maintains the structural integrity of full-length satellite RNA.
- Mechanism The SPMV capsid protein has multiple functions associated with pathogenesis in infected millet.