TST (gene)

Thiosulfate sulfurtransferase is an enzyme that in humans is encoded by the TST gene.^[5][6]

TST
Identifiers
Aliases	TST, RDS, thiosulfate sulfurtransferase
External IDs	OMIM: 180370; MGI: 98852; HomoloGene: 37759; GeneCards: TST; OMA:TST - orthologs
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q12.3 Start 37,010,859 bp[1] End 37,020,183 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 E1|15 37.47 cM Start 78,283,756 bp[2] End 78,290,107 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon right lobe of liver mucosa of sigmoid colon mucosa of ileum right adrenal cortex jejunal mucosa duodenum left adrenal gland left adrenal cortex kidney tubule Top expressed in olfactory epithelium left lobe of liver pyloric antrum gastric mucosa mucous cell of stomach epithelium of stomach esophagus adrenal gland left colon optic nerve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity 5S rRNA binding thiosulfate sulfurtransferase activity RNA binding Cellular component mitochondrial inner membrane extracellular exosome mitochondrion mitochondrial matrix extracellular space Biological process rRNA transport rRNA import into mitochondrion epithelial cell differentiation cyanate catabolic process sulfur amino acid catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7263 22117 Ensembl ENSG00000128311 ENSMUSG00000044986 UniProt Q16762 P52196 RefSeq (mRNA) NM_003312 NM_001270483 NM_009437 RefSeq (protein) NP_001257412 NP_003303 NP_033463 Location (UCSC) Chr 22: 37.01 – 37.02 Mb Chr 15: 78.28 – 78.29 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000128311 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000044986 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Pallini R, Guazzi GC, Cannella C, Cacace MG (Dec 1991). "Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes". Biochem Biophys Res Commun. 180 (2): 887–93. doi:10.1016/S0006-291X(05)81148-9. PMID 1953758.
6. "Entrez Gene: TST thiosulfate sulfurtransferase (rhodanese)".

Further reading

• Pecci L, Pensa B, Costa M, et al. (1976). "Reaction of rhodanese with dithiothreitol". Biochim. Biophys. Acta. 445 (1): 104–11. doi:10.1016/0005-2744(76)90163-7. PMID 986188.
• Polo CF, Vazquez ES, Caballero F, et al. (1993). "Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation". Comp. Biochem. Physiol. B. 103 (1): 251–6. doi:10.1016/0305-0491(92)90440-3. PMID 1451437.
• Lewis JL, Rhoades CE, Gervasi PG, et al. (1991). "The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa". Toxicol. Appl. Pharmacol. 108 (1): 114–20. doi:10.1016/0041-008X(91)90274-I. PMID 2006499.
• Malliopoulou VA, Rakitzis ET, Malliopoulou TB (1989). "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. PMID 2817794.
• Vazquez E, Buzaleh AM, Wider E, Batlle AM (1987). "Red blood cell rhodanese: its possible role in modulating delta-aminolaevulinate synthetase activity in mammals". Int. J. Biochem. 19 (2): 217–9. doi:10.1016/0020-711X(87)90337-5. PMID 3471602.
• Pallini R, Martelli P, Bardelli AM, et al. (1987). "Normal rhodanese activity in leukocytes from Leber patients: enzyme characterization and activity levels". Neurology. 37 (12): 1878–80. doi:10.1212/wnl.37.12.1878. PMID 3479705. S2CID 35839633.
• Pagani S, Galante YM (1983). "Interaction of rhodanese with mitochondrial NADH dehydrogenase". Biochim. Biophys. Acta. 742 (2): 278–84. doi:10.1016/0167-4838(83)90312-6. PMID 6402020.
• Mimori Y, Nakamura S, Kameyama M (1984). "Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system". J. Neurochem. 43 (2): 540–5. doi:10.1111/j.1471-4159.1984.tb00932.x. PMID 6588145. S2CID 10055954.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Merrill GA, Butler M, Horowitz PM (1993). "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. doi:10.1016/S0021-9258(18)82300-6. PMID 8340386.
• Aita N, Ishii K, Akamatsu Y, et al. (1997). "Cloning and expression of human liver rhodanese cDNA". Biochem. Biophys. Res. Commun. 231 (1): 56–60. doi:10.1006/bbrc.1996.6046. PMID 9070219.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
• Wieprecht T, Apostolov O, Beyermann M, Seelig J (2001). "Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation". Biochemistry. 39 (50): 15297–305. doi:10.1021/bi001774v. PMID 11112515.
• Picton R, Eggo MC, Merrill GA, et al. (2002). "Mucosal protection against sulphide: importance of the enzyme rhodanese". Gut. 50 (2): 201–5. doi:10.1136/gut.50.2.201. PMC 1773108. PMID 11788560.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Kwiecień I, Sokołowska M, Luchter-Wasylewska E, Włodek L (2004). "Inhibition of the catalytic activity of rhodanese by S-nitrosylation using nitric oxide donors". Int. J. Biochem. Cell Biol. 35 (12): 1645–57. doi:10.1016/S1357-2725(03)00005-0. PMID 12962704.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.