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TST thiosulfate sulfurtransferase (rhodanese)

Thiosulfate Sulfurtransferase
This is one of two neighboring genes encoding similar proteins that each contain two rhodanese domains. The encoded protein is localized to the mitochondria and catalyzes the conversion of thiosulfate and cyanide to thiocyanate and sulfite. In addition, the protein interacts with 5S ribosomal RNA and facilitates its import into the mitochondria. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012] (from NCBI)
Top mentioned proteins: CAN, ACID, fibrillin-1, Inactive, CIs
Papers on Thiosulfate Sulfurtransferase
Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA.
Giedroc et al., Bloomington, United States. In Biochemistry, May 2015
The N-terminal domain of CstA exhibits thiosulfate sulfurtransferase (TST; rhodanese) activity, and a Cys66 (34)S-persulfide is formed as a catalytic intermediate in both the presence and absence of the adjacent TusA-like domain using (34)S-SO3(2-) as a substrate.
Mechanisms on boron-induced alleviation of aluminum-toxicity in Citrus grandis seedlings at a transcriptional level revealed by cDNA-AFLP analysis.
Chen et al., Fuzhou, China. In Plos One, 2014
Results showed that genes related to detoxification of reactive oxygen species (ROS) and aldehydes (i.e., glutathione S-transferase zeta class-like isoform X1, thioredoxin M-type 4, and 2-alkenal reductase (NADP+-dependent)-like), metabolism (i.e., carboxylesterases and lecithin-cholesterol acyltransferase-like 4-like, nicotianamine aminotransferase A-like isoform X3, thiosulfate sulfurtransferase 18-like isoform X1, and FNR, root isozyme 2), cell transport (i.e., non-specific lipid-transfer protein-like protein At2g13820-like and major facilitator superfamily protein), Ca signal and hormone (i.e., calcium-binding protein CML19-like and IAA-amino acid hydrolase ILR1-like 4-like), gene regulation (i.e., Gag-pol polyprotein) and cell wall modification (i.e., glycosyl hydrolase family 10 protein) might play a role in B-induced alleviation of Al-toxicity.
Roles of Sulfur Metabolism and Rhodanese in Detoxification and Anti-Oxidative Stress Functions in the Liver: Responses to Radiation Exposure.
Nakajima, Chiba, Japan. In Med Sci Monit, 2014
The detoxification enzyme rhodanese, which is also called thiosulfate sulfurtransferase (TST), has been demonstrated to be induced in the liver in response to radiation.
Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine λ-lyase activities.
Bhattacharya et al., Gwalior, India. In J Biochem Mol Toxicol, 2013
We assessed the dose-dependent effect of potassium cyanide (KCN) on thiosulfate sulfurtransferase (TST), 3-mercaptopyruvate sulfurtransferase (3-MPST), and cystathionine λ-lyase (CST) activities in mice.
Decreased mucosal sulfide detoxification is related to an impaired butyrate oxidation in ulcerative colitis.
Verbeke et al., Leuven, Belgium. In Inflamm Bowel Dis, 2012
The colonic mucosal thiosulfate sulfurtransferase (TST) enzyme removes H(2) S by conversion to the less toxic thiocyanate.
Feeding low or pharmacological concentrations of zinc oxide changes the hepatic proteome profiles in weaned piglets.
Einspanier et al., Berlin, Germany. In Plos One, 2012
arginase1, thiosulfate sulfurtransferase, HSP70) and 8 up-regulated (e.g.
Protective effect of Phellinus linteus polysaccharide extracts against thioacetamide-induced liver fibrosis in rats: a proteomics analysis.
Wan et al., Hong Kong, Hong Kong. In Chin Med, 2011
A total of 13 differentially expressed proteins including actin, tubulin alpha-1C chain, preprohaptoglobin, hemopexin, galectin-5, glutathione S-transferase alpha-4 (GSTA4), branched chain keto acid dehydrogenase hterotetrameric E1 subunit alpha (BCKDHA), glutathione S-transferase mu (GSTmu); glyceraldehyde-3-phosphate dehydrogenase (GAPDH); thiosulfate sulfurtransferase (TFT); betaine-homocysteine S-methyltransferase 1 (BHMT1); quinoid dihydropteridine reductase (QDPR); ribonuclease UK114 were observed between the TAA and PLP groups.
Analysis of intracellular expressed proteins of Mycobacterium tuberculosis clinical isolates.
Bisht et al., Āgra, India. In Proteome Sci, 2011
Four proteins (adenosylhomocysteinase, aspartate carbomyltransferase, putatitive thiosulfate sulfurtransferase and universal stress protein) were present in both intracellular MDR and sensitive isolates and three of these belonged to intermediary metabolism and respiration category.
A rhodanese-like protein is highly overrepresented in the mutant S. clavuligerus oppA2::aph: effect on holomycin and other secondary metabolites production.
Liras et al., León, Spain. In Microb Biotechnol, 2011
A protein highly overrepresented in the proteome of Streptomyces clavuligerus oppA2::aph was characterized by MS/MS as a rhodanese-like enzyme.
Catalytic site cysteines of thiol enzyme: sulfurtransferases.
Nagahara, Tokyo, Japan. In J Amino Acids, 2010
In particular, oxidized forms of sulfurtransferases, such as mercaptopyruvate sulfurtransferase and thiosulfate sulfurtransferase, are not reduced by reduced glutathione but by reduced thioredoxin.
Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import into human mitochondria.
Tarassov et al., Strasbourg, France. In J Biol Chem, 2010
silencing of the rhodanese gene caused not only a proportional decrease of 5 S rRNA import but also a general inhibition of mitochondrial translation, indicating the functional importance of the imported 5 S rRNA inside the organelle.
Identification of Rack1, EF-Tu and Rhodanese as aging-related proteins in human colonic epithelium by proteomic analysis.
Xiao et al., Changsha, China. In J Proteome Res, 2010
Proteomics was used to study colonic epithelial aging, for differential proteins in the human normal colonic epithelial tissues from young and old people. Rack1, EF-Tu and Rhodanese, three validated differential proteins, were further investigated.
Low expression of thiosulfate sulfurtransferase (rhodanese) predicts mortality in hemodialysis patients.
Scholze et al., Berlin, Germany. In Clin Biochem, 2010
OBJECTIVES: To test the hypothesis that impaired expression of the thiosulfate sulfurtransferase rhodanese is associated with oxidative stress and may predict mortality in hemodialysis patients.
Induction of rhodanese, a detoxification enzyme, in livers from mice after long-term irradiation with low-dose-rate gamma-rays.
Nenoi et al., Chiba, Japan. In J Radiat Res (tokyo), 2008
One of the proteins that showed marked changes in expression was identified as rhodanese (thiosulfate sulfurtransferase).
Expression, purification, crystallization and preliminary X-ray analysis of Rv3117, a probable thiosulfate sulfurtransferase (CysA3) from Mycobacterium tuberculosis.
James et al., Edmonton, Canada. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008
The gene product of open reading frame Rv3117 from Mycobacterium tuberculosis (Mtb) strain H37Rv is annotated as encoding a probable rhodanese-like thiosulfate sulfurtransferase (MtbCysA3).
Age-related changes in the activity of cerebral rhodanese in mice during the first four months of life.
Ben-Attia et al., Bizerte, Tunisia. In Brain Dev, 2008
increased sensitivity to cyanide, generally reported in old mice, may be due in part to a decrease in the activity of brain rhodanese
Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8).
Dhe-Paganon et al., Toronto, Canada. In J Biol Chem, 2007
The USP8 recognition domain of NRDP1 has a novel protein fold that interacts with a conserved peptide loop of the rhodanese domain.
Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.
Leimkühler et al., Braunschweig, Germany. In Biochemistry, 2005
A partially gluconoylated N-terminus of the His6-tagged molybdenum cofactor synthesis 3 (MOCS3)-rhodanese-like domain is identified which results in a heterogeneity of the protein but does not influence sulfurtransferase activity.
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