Biology:TST (gene)

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Thiosulfate sulfurtransferase is an enzyme that in humans is encoded by the TST gene.

The product of this gene is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes.

The gene product contains two highly conservative domains (rhodanese homology domains), suggesting these domains have a common evolutionary origin.

Further reading

• "Reaction of rhodanese with dithiothreitol". Biochim. Biophys. Acta 445 (1): 104–11. 1976. doi:10.1016/0005-2744(76)90163-7. PMID 986188. 
• "Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation". Comp. Biochem. Physiol. B 103 (1): 251–6. 1993. doi:10.1016/0305-0491(92)90440-3. PMID 1451437. 
• "The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa". Toxicol. Appl. Pharmacol. 108 (1): 114–20. 1991. doi:10.1016/0041-008X(91)90274-I. PMID 2006499. 
• "Inactivation of rhodanese from human gastric mucosa and stomach adenocarcinoma by 2,4, 6-trinitrobenzenesulphonate and by 4,4'-diisothiocyanatostilbene-2,2'-disulphonate". Anticancer Res. 9 (4): 1133–6. 1989. PMID 2817794. 
• "Red blood cell rhodanese: its possible role in modulating delta-aminolaevulinate synthetase activity in mammals". Int. J. Biochem. 19 (2): 217–9. 1987. doi:10.1016/0020-711X(87)90337-5. PMID 3471602. 
• "Normal rhodanese activity in leukocytes from Leber patients: enzyme characterization and activity levels". Neurology 37 (12): 1878–80. 1987. doi:10.1212/wnl.37.12.1878. PMID 3479705. 
• "Interaction of rhodanese with mitochondrial NADH dehydrogenase". Biochim. Biophys. Acta 742 (2): 278–84. 1983. doi:10.1016/0167-4838(83)90312-6. PMID 6402020. 
• "Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system". J. Neurochem. 43 (2): 540–5. 1984. doi:10.1111/j.1471-4159.1984.tb00932.x. PMID 6588145. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding". J. Biol. Chem. 268 (21): 15611–20. 1993. doi:10.1016/S0021-9258(18)82300-6. PMID 8340386. 
• "Cloning and expression of human liver rhodanese cDNA". Biochem. Biophys. Res. Commun. 231 (1): 56–60. 1997. doi:10.1006/bbrc.1996.6046. PMID 9070219. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. 1999. doi:10.1038/990031. PMID 10591208. Bibcode: 1999Natur.402..489D. 
• "Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation". Biochemistry 39 (50): 15297–305. 2001. doi:10.1021/bi001774v. PMID 11112515. 
• "Mucosal protection against sulphide: importance of the enzyme rhodanese". Gut 50 (2): 201–5. 2002. doi:10.1136/gut.50.2.201. PMID 11788560. 
• "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. 2004. doi:10.1038/nbt810. PMID 12665801. 
• "Inhibition of the catalytic activity of rhodanese by S-nitrosylation using nitric oxide donors". Int. J. Biochem. Cell Biol. 35 (12): 1645–57. 2004. doi:10.1016/S1357-2725(03)00005-0. PMID 12962704. 
• "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.