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Gene Review

C10orf32  -  chromosome 10 open reading frame 32

Homo sapiens

Synonyms: FLJ40752, UPF0693 protein C10orf32
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High impact information on C10orf32

  • Together these results suggest a mechanism for CYT-19 and other general DExD/H-box RNA chaperones in which the proteins bind to structured RNAs and efficiently unwind loosely associated duplexes, which biases the proteins to disrupt nonnative base pairs and gives the liberated strands an opportunity to refold [1].
  • Furthermore, CYT-19 performs this reaction 50-fold more efficiently than it unwinds the same duplex free in solution, suggesting that it forms additional interactions with the ribozyme, most likely using a distinct RNA binding site from the one responsible for unwinding [1].
  • We set out to study the pharmacogenetics of human arsenic methyltransferase (AS3MT, previously CYT19) [2].
  • Previous studies showed that purified CYT-19 stimulates the in vitro splicing of structurally diverse group I and group II introns, and uses the energy of ATP binding or hydrolysis to resolve kinetic traps [3].
  • We report the results of a screen for genetic association with urinary arsenic metabolite levels in three arsenic metabolism candidate genes, PNP, GSTO, and CYT19, in 135 arsenic-exposed subjects from the Yaqui Valley in Sonora, Mexico, who were exposed to drinking water concentrations ranging from 5.5 to 43.3 ppb [4].

Biological context of C10orf32

  • Here, we compare the effects of sodium selenite and mono-, di-, and trimethylated selenium compounds on the methylation of arsenite by purified recombinant rat As(III)-methyltransferase (Cyt19) and by primary rat and human hepatocytes [5].
  • Subsequent analysis of this association revealed that the association signal for the entire population was actually caused by an extremely strong association in only the children (7-11 years of age) between CYT19 genotype and D:M levels [4].
  • The existence of a strong, developmentally regulated genetic association between CYT19 and arsenic metabolism carries import for both arsenic pharmacogenetics and arsenic toxicology, as well as for public health and governmental regulatory officials [4].
  • This 42-kDa protein has sequence motifs common to many non-nucleic acid methyltransferases and is closely related to methyltransferases of previously unknown function that have been identified by conceptual translations of cyt19 genes of mouse and human genomes [6].
  • Analysis of the coding sequence of cyt19 identified one heterozygote with Met287Thr mutation in a single allele [7].

Associations of C10orf32 with chemical compounds

  • Our studies with recombinant rat cyt19 find that, in the presence of an exogenous or a physiological reductant, this protein can catalyze the entire sequence of reactions that convert arsenite to methylated metabolites [6].
  • A scheme linking cyt19 and thioredoxin-thioredoxin reductase in the methylation and reduction of arsenicals is proposed [6].


  1. Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone. Tijerina, P., Bhaskaran, H., Russell, R. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies. Wood, T.C., Salavagionne, O.E., Mukherjee, B., Wang, L., Klumpp, A.F., Thomae, B.A., Eckloff, B.W., Schaid, D.J., Wieben, E.D., Weinshilboum, R.M. J. Biol. Chem. (2006) [Pubmed]
  3. Involvement of DEAD-box Proteins in Group I and Group II Intron Splicing. Biochemical Characterization of Mss116p, ATP Hydrolysis-dependent and -independent Mechanisms, and General RNA Chaperone Activity. Halls, C., Mohr, S., Del Campo, M., Yang, Q., Jankowsky, E., Lambowitz, A.M. J. Mol. Biol. (2007) [Pubmed]
  4. Developmentally restricted genetic determinants of human arsenic metabolism: association between urinary methylated arsenic and CYT19 polymorphisms in children. Meza, M.M., Yu, L., Rodriguez, Y.Y., Guild, M., Thompson, D., Gandolfi, A.J., Klimecki, W.T. Environ. Health Perspect. (2005) [Pubmed]
  5. Selenium compounds modulate the activity of recombinant rat AsIII-methyltransferase and the methylation of arsenite by rat and human hepatocytes. Walton, F.S., Waters, S.B., Jolley, S.L., LeCluyse, E.L., Thomas, D.J., Styblo, M. Chem. Res. Toxicol. (2003) [Pubmed]
  6. Elucidating the pathway for arsenic methylation. Thomas, D.J., Waters, S.B., Styblo, M. Toxicol. Appl. Pharmacol. (2004) [Pubmed]
  7. Interindividual variation in the metabolism of arsenic in cultured primary human hepatocytes. Drobná, Z., Waters, S.B., Walton, F.S., LeCluyse, E.L., Thomas, D.J., Stýblo, M. Toxicol. Appl. Pharmacol. (2004) [Pubmed]
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