Feb 15, 2020 · Owing to the similarity between the ionic hydrated radius of Cd 2+ and Fe 2+, this study investigated how the Cd tolerance and accumulation of Arabidopsis plants was affected by the knockdown of BTS, a gene that negatively regulates Fe nutrition.

Encodes BRUTUS (BTS), a putative E3 ligase protein with metal ion binding and DNA binding domains, which negatively regulates the response to iron deficiency.

Additionally, we identified a novel allele of BTS in a mutagenesis screen for altered Fe accumulation. This mutant, bts-3, contains a point mutation in the RING E3 ligase domain of BTS, suggesting its E3 ligase activity may be impaired.

Jan 30, 2022 · Here, we showed that the T-DNA insertion-induced inhibition of the BRUTUS (BTS) gene in the bts-1 mutant greatly improved Zn tolerance, as indicated by increased biomass production and reduced leaf chlorosis.

Jul 19, 2017 · The Arabidopsis thaliana E3 ligase BRUTUS (BTS) is involved in the negative regulation of the Fe deficiency response and we show here that the two A. thaliana BTS …

Feb 15, 2020 · Owing to the similarity between the ionic hydrated radius of Cd 2+ and Fe 2+, this study investigated how the Cd tolerance and accumulation of Arabidopsis plants was affected by the knockdown of BTS, a gene that negatively regulates Fe nutrition.

Sep 18, 2024 · Encodes BRUTUS (BTS), a putative E3 ligase protein with metal ion binding and DNA binding domains, which negatively regulates the response to iron deficiency.

Encodes BRUTUS (BTS), a putative E3 ligase protein with metal ion binding and DNA binding domains, which negatively regulates the response to iron deficiency. The mRNA is cell-to-cell mobile.

Nov 20, 2013 · The closest homologue of OsHRZ1 and OsHRZ2 in Arabidopsis was found to be BTS (Fig. 1), which was previously identified as an Fe deficiency-induced gene expressed predominantly in the pericycle...

Jun 16, 2017 · Additionally, we identified a novel allele of BTS in a mutagenesis screen for altered Fe accumulation. This mutant, bts-3, contains a point mutation in the RING E3 ligase domain of BTS, suggesting its E3 ligase activity may be impaired.