Claim · model-written summary
Mutations of HSR201 did not affect its protein stability or activity.
- Taxon
- Nicotiana benthamiana
Nicotiana benthamianae2 - Treatment
- mutationse1
- Gene
- HSR201e1
- Outcome
- protein stability or activitye1
- Direction
- did not affecte1
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“these mutations did not affect the protein stability or activity of HSR201”
e2“The virus-induced gene silencing (VIGS) of PEX5, a PTS1 receptor, but not PEX7, a PTS2 receptor, compromised the peroxisomal targeting of HSR201 in Nicotiana benthamiana”
Title
Yu Kotera; Yoshika Asai; Shutaro Okano; et al. Plant and Cell Physiology 2024. doi:10.1093/pcp/pcae129
Other claims from this paper (12)
- Observation HSR201 fused to a yellow fluorescent protein localized in peroxisomes in Nicotiana benthamiana.
- Observation A bioinformatics analysis failed to identify PTS1- or PTS2-like signals for HSR201.
- Intervention effect Deletion and mutation analyses identified the extreme C-terminal Leu460 as an essential residue for peroxisomal localization of HSR201.
- Intervention effect Deletion and mutation analyses identified Ile455, Ile456 and Ala459 as important residues for peroxisomal localization of HSR201.
- Intervention effect VIGS of PEX5, a PTS1 receptor, compromised peroxisomal targeting of HSR201 in Nicotiana benthamiana.
- Intervention effect VIGS of PEX7, a PTS2 receptor, did not compromise peroxisomal targeting of HSR201 in Nicotiana benthamiana.
- Intervention effect HSR201 mutants with reduced or non-peroxisomal targeting induced lower SA levels than the wild type when overexpressed with NtCNL in tobacco.
- Intervention effect VIGS of the HSR201 homolog compromised pathogen signal-induced SA accumulation in N. benthamiana.
- Intervention effect The HSR201 wild type complemented the pathogen signal-induced SA accumulation lost in VIGS plants.
- Intervention effect The mutant with non-peroxisomal targeting did not complement the pathogen signal-induced SA accumulation of VIGS plants.
- Mechanism Peroxisomal localization of HSR201 is suggested to be mediated by a non-canonical PTS1.
- Mechanism Peroxisomal localization of HSR201 is suggested to be required for SA biosynthesis.