Advanced SearchSearch Tips
Reactive oxygen species-dependent down-regulation of ubiquitin C-terminal hydrolase in Schizosaccharomyces pombe
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Reactive oxygen species-dependent down-regulation of ubiquitin C-terminal hydrolase in Schizosaccharomyces pombe
Jo, Hannah; Lim, Hye-Won; Kwon, Hee-Souk; Lim, Chang-Jin; Park, Kwang Hark; Jin, Chang Duck; Kim, Kyunghoon;
  PDF(new window)
The Schizosaccharomyces pombe gene, belonging to the PPPDE superfamily of deubiquitinating enzyme (DUB) genes, was previously shown to encode a protein with ubiquitin C-terminal hydrolase (UCH) activity and to participate in the response against oxidative and nitrosative stresses. This work focused on the reactive oxygen species (ROS)-dependent regulation of the S. pombe gene. UCH activities, encoded by the gene, were attenuated in the S. pombe cells exposed to , superoxide radical-generating menadione (MD), and nitric oxide (NO)-generating sodium nitroprusside (SNP). Reduced glutathione (GSH) and its precursor N-acetylcysteine (NAC) were able to significantly enhance the UCH activities in the absence or presence of . However, the influences of both GSH and NAC on the ROS levels in the absence or presence of were opposite to their effects on the UCH activities under the same conditions. The UCH activities in the Sdu1-overexpressing S. pombe cells were also diminished under exposure to , MD and SNP, but still remained to be higher than those in the vector control cells. In brief, it is proposed that the S. pombe gene is regulated by ROS in a negative manner, the meaning of which largely remains elusive.
;Schizosaccharomyces pombe;deubiquitinating enzyme;reactive oxygen species;ubiquitin C-terminal hydrolase;
 Cited by
Bheda, A., Shackelford, J., and Pagano, J.S. 2009. Expression and functional studies of ubiquitin C-terminal hydrolase L1 regulated genes. PLoS One 4, e6764. crossref(new window)

Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254. crossref(new window)

Carolan, B.J., Heguy, A., Harvey, B.G., Leopold, P.L., Ferris, B., and Crystal, R.G. 2006. Up-regulation of expression of the ubiquitin carboxyl-terminal hydrolase L1 gene in human airway epithelium of cigarette smokers. Cancer Res. 66, 10729-10740. crossref(new window)

Colland, F. 2010. The therapeutic potential of deubiquitinating enzyme inhibitors. Biochem. Soc. Trans. 38(Pt 1), 137-143. crossref(new window)

Cotto-Rios, X.M., Bekes, M., Chapman, J., Ueberheide, B., and Huang, T.T. 2012. Deubiquitinases as a signaling target of oxidative stress. Cell Rep. 2, 1475-1484. crossref(new window)

Eletr, Z.M. and Wilkinson, K.D. 2014. Regulation of proteolysis by human deubiquitinating enzymes. Biochim. Biophys. Acta 1843, 114-128. crossref(new window)

Iyer, L.M., Koonin, E.V., and Aravind, L. 2004. Novel predicted peptidases with a potential role in the ubiquitin signaling pathway. Cell Cycle 3, 1440-1450. crossref(new window)

Johnston, S.C., Riddle, S.M., Cohen, R.E., and Hill, C.P. 1999. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18, 3877-3887. crossref(new window)

Kiani-Esfahani, A., Tavalaee, M., Deemeh, M.R., Hamiditabar, M., and Nasr-Esfahani, M.H. 2012. DHR123: an alternative probe for assessment of ROS in human spermatozoa. Syst. Biol. Reprod. Med. 58, 168-174. crossref(new window)

Kim, Y., Jo, H., and Lim, C.J. 2013. Deubiquitinating activity of Sdu1, a putative member of the PPPDE peptidase family, in Schizosaccharomyces pombe. Can. J. Microbiol. 59, 789-796. crossref(new window)

Kim, J.H., Park, K.C., Chung, S.S., Bang, O., and Chung, C.H. 2003. Deubiquitinating enzymes as cellular regulators. J. Biochem. 134, 9-18. crossref(new window)

Komander, D., Clague, M.J., and Urbe, S. 2009. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell. Biol. 10, 550-563. crossref(new window)

Liu, Y., Lashuel, H.A., Choi, S., Xing, X., Case, A., Ni, J., Yeh, L.A., Cuny, G.D., Stein, R.L., and Lansbury, P.T.Jr. 2003. Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line. Chem. Biol. 10, 837-846. crossref(new window)

Maiti, T.K., Permaul, M., Boudreaux, D.A., Mahanic, C., Mauney, S., and Das, C. 2011. Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme. FEBS J. 278, 4917-4926. crossref(new window)

Myers, A.M., Tzagoloff, A., Kinney, D.M., and Lusty, C.J. 1986. Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions. Gene 45, 299-310. crossref(new window)

Ramakrishna, S., Suresh, B., and Baek, K.H. 2011. The role of deubiquitinating enzymes in apoptosis. Cell. Mol. Life Sci. 68, 15-26. crossref(new window)

Reyes-Turcu, F.E., Ventii, K.H., and Wilkinson, K.D. 2009. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 78, 363-397. crossref(new window)

Rolfe, M., Chiu, M.I., and Pagano, M. 1997. The ubiquitin-mediated proteolytic pathway as a therapeutic area. J. Mol. Med. (Berl) 75, 5-17. crossref(new window)

Royall, J.A. and Ischiropoulos, H. 1993. Evaluation of 2',7'-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular $H_2O_2$ in cultured endothelial cells. Arch. Biochem. Biophys. 302, 348-355. crossref(new window)

Satoh, J.I. and Kuroda, Y. 2001. Ubiquitin C-terminal hydrolase-L1 (PGP9.5) expression in human neural cell lines following induction of neuronal differentiation and exposure to cytokines, neurotrophic factors or heat stress. Neuropathol. Appl. Neurobiol. 27, 95-104. crossref(new window)

Shen, H., Sikorska, M., Leblanc, J., Walker, P.R., and Liu, Q.Y. 2006. Oxidative stress regulated expression of ubiquitin Carboxylterminal Hydrolase-L1: role in cell survival. Apoptosis 11, 1049-1059. crossref(new window)

Todi, S.V., Winborn, B.J., Scaglione, K.M., Blount, J.R., Travis, S.M., and Paulson, H.L. 2009. Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. EMBO J. 28, 372-382. crossref(new window)

Tse, W.K., Eisenhaber, B., Ho, S.H., Ng, Q., Eisenhaber, F., and Jiang, Y.J. 2009. Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development. BMC Genomics 10, 637. crossref(new window)

Wolberger, C. 2014. Mechanisms for regulating deubiquitinating enzymes. Protein Sci. 23, 344-353. crossref(new window)

Yi, Y.J., Manandhar, G., Sutovsky, M., Li, R., Jonakova, V., Oko, R., Park, C.S., Prather, R.S., and Sutovsky, P. 2007. Ubiquitin C-terminal hydrolase-activity is involved in sperm acrosomal function and anti-polyspermy defense during porcine fertilization. Biol. Reprod. 77, 780-793. crossref(new window)

Yin, S.T., Huang, H., Zhang, Y.H., Zhou, Z.R., Song, A.X., Hong, F.S., and Hu, H.Y. 2011. A fluorescence assay for elucidating the substrate specificities of deubiquitinating enzymes. Biochem. Biophys. Res. Commun. 416, 76-79. crossref(new window)