Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Arabidopsis mutants in the C-S lyase of glucosinolate biosynthesis establish a critical role for indole-3-acetaldoxime in auxin homeostasis.
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SUR1 is the glucosinolate C-S lyase; sur1 lacks aliphatic and indole glucosinolates, accumulates C-S lyase substrate, and its high-auxin phenotype arises from IAOx diversion into IAA.
"We report characterization of SUPERROOT1 (SUR1) as the C-S lyase in glucosinolate biosynthesis."
Auxin, ethylene and brassinosteroids: tripartite control of growth in the Arabidopsis hypocotyl.
Proteomic analysis of different mutant genotypes of Arabidopsis led to the identification of 11 proteins correlating with adventitious root development.
A novel C-S lyase from the latex-producing plant Taraxacum brevicorniculatum displays alanine aminotransferase and l-cystine lyase activity.
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A SUR1-homologous PLP C-S lyase from Taraxacum is cytosolic, has L-cystine lyase and AlaAT but no TyrAT activity.
"However, we detected no in vitro tyrosine aminotransferase (TyrAT) activity"
A proteomic strategy for global analysis of plant protein complexes.
Global Analysis of Membrane-associated Protein Oligomerization Using Protein Correlation Profiling.
REVERSAL OF RDO5 1, a Homolog of Rice Seed Dormancy4, Interacts with bHLH57 and Controls ABA Biosynthesis and Seed Dormancy in Arabidopsis.
Extensive signal integration by the phytohormone protein network.
SUPERROOT1 is not the only C-S lyase capable to contribute to glucosinolate biosynthesis in Arabidopsis thaliana.
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sur1 retains significant indolic glucosinolates, implying an additional C-S lyase; elevated auxin in sur1 depends on MYB34.
"we show that elevated auxin production in the sur1 plant depends on the MYB34 transcription factor"
Superroot, a recessive mutation in Arabidopsis, confers auxin overproduction.
Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis.