Exogenous Sulfide Reverses the Alteration of Transcriptional Profiling of the des1-1 Mutant (Arabidopsis thaliana)

ABSTRACT: Arabidopsis thaliana cells contain different O-acetylserine(thiol)lyase (OASTL) enzymes that catalyze the biosynthesis of cysteine. Recently, we have deeply investigated about one of the minor OASTL-like protein located in the cytosol, named DES1, highlighting some important clues about its metabolic function. We have demonstrated that DES1 catalyzes the desulfuration of L-cysteine to sulfide plus ammonia and pyruvate, instead of the biosynthesis of Cys, and thus, is a novel L-cysteine desulfhydrase (EC 4.4.1.1). The functionality of DES1 is being revealed by the phenotype of the T-DNA insertion mutants des1-1 and des1-2. We have performed a comparative transcriptomic analysis on leaves of the des1-1 and Col-0 wild type plants grown for 30 days under long-day conditions. The normalized dat

ORGANISM(S): Arabidopsis thaliana

SUBMITTER: Cecilia Gotor 

PROVIDER: E-GEOD-32566 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress