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Mol. Cells 2012; 34(2): 209-218

Published online August 31, 2012

https://doi.org/10.1007/s10059-012-0155-6

© The Korean Society for Molecular and Cellular Biology

Two Thioredoxin Reductases, trxr-1 and trxr-2, Have Differential Physiological Roles in Caenorhabditis elegans

Weixun Li1,2, Jaya Bandyopadhyay3, Hyun Sook Hwaang4,5, Byung-Jae Park6, Jeong Hoon Cho7, Jin Il Lee8, Joohong Ahnn1,2,9,*, and Sun-Kyung Lee1,9,*

1Department of Life Science, Hanyang University, Seoul 133-791, Korea, 2Brain Korea 21 Life Science for Global Warming Team, Hanyang University, Seoul 133-791, Korea, 3Department of Biotechnology, West Bengal University of Technology, Kolkata 700-064, India, 4Department of Bioengineering, Hanyang University, Seoul 133-791, Korea, 5Department of Chemistry, Hanyang University, Seoul 133-791, Korea, 6Department of Life Science, Hallym University, Chunchon 200-702, Korea, 7Division of Biology Education, College of Education, Chosun University, Gwangju 501-759, Korea, 8Fred Hutchinson Cancer Research Center, Basic Sciences Division, 1100 Fairview Ave. N. Seattle, WA 98109, USA, 9The Research Institute for Natural Sciences, Hanyang University, Seoul 133-791, Korea

Correspondence to : *Correspondence: sunkyungl@hanyang.ac.kr (SKL); joohong@hanyang.ac.kr (JA)

Received: June 5, 2012; Revised: July 3, 2012; Accepted: July 4, 2012

Abstract

Thioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide reductase family, which mainly func-tions in the thioredoxin system. TrxR is found in all living organisms and exists in two major ubiquitous isoen-zymes in higher eukaryotic cells; One is cytosolic and the other mitochondrial. Mitochondrial TrxR functions to protect mitochondria from oxidative stress, where reactive oxidative species are mainly generated, while cytosolic TrxR plays a role to maintain optimal oxido-reductive status in cytosol. In this study, we report differential physiological functions of these two TrxRs in C. elegans. trxr-1, the cytosolic TrxR, is highly expressed in pharynx, vulva and intestine, whereas trxr-2, the mitochondrial TrxR, is mainly expressed in pharyngeal and body wall muscles. Deficiency of the non-selenoprotein trxr-2 caused defects in longevity and delayed development under stress conditions, while deletion mutation of the selenoprotein trxr-1 resulted in interference in acidification of lysosomal compartment in intestine. Interestingly, the acidification defect of trxr-1(jh143) deletion mutant was rescued, not only by selenocystein-containing wild type TRXR-1, but also cysteine-substituted mutant TRXR-1. Both trxr-1 and trxr-2 were up-regulated when worms were challenged by environmental stress such as heat shock. These results suggest that trxr-1 and trxr-2 function differently at organismal level presumably by their differential sub-cellular localization in C. elegans.

Keywords C. elegans, longevity, oxidative stress, thioredoxin reductase, V-ATPase

Article

Research Article

Mol. Cells 2012; 34(2): 209-218

Published online August 31, 2012 https://doi.org/10.1007/s10059-012-0155-6

Copyright © The Korean Society for Molecular and Cellular Biology.

Two Thioredoxin Reductases, trxr-1 and trxr-2, Have Differential Physiological Roles in Caenorhabditis elegans

Weixun Li1,2, Jaya Bandyopadhyay3, Hyun Sook Hwaang4,5, Byung-Jae Park6, Jeong Hoon Cho7, Jin Il Lee8, Joohong Ahnn1,2,9,*, and Sun-Kyung Lee1,9,*

1Department of Life Science, Hanyang University, Seoul 133-791, Korea, 2Brain Korea 21 Life Science for Global Warming Team, Hanyang University, Seoul 133-791, Korea, 3Department of Biotechnology, West Bengal University of Technology, Kolkata 700-064, India, 4Department of Bioengineering, Hanyang University, Seoul 133-791, Korea, 5Department of Chemistry, Hanyang University, Seoul 133-791, Korea, 6Department of Life Science, Hallym University, Chunchon 200-702, Korea, 7Division of Biology Education, College of Education, Chosun University, Gwangju 501-759, Korea, 8Fred Hutchinson Cancer Research Center, Basic Sciences Division, 1100 Fairview Ave. N. Seattle, WA 98109, USA, 9The Research Institute for Natural Sciences, Hanyang University, Seoul 133-791, Korea

Correspondence to:*Correspondence: sunkyungl@hanyang.ac.kr (SKL); joohong@hanyang.ac.kr (JA)

Received: June 5, 2012; Revised: July 3, 2012; Accepted: July 4, 2012

Abstract

Thioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide reductase family, which mainly func-tions in the thioredoxin system. TrxR is found in all living organisms and exists in two major ubiquitous isoen-zymes in higher eukaryotic cells; One is cytosolic and the other mitochondrial. Mitochondrial TrxR functions to protect mitochondria from oxidative stress, where reactive oxidative species are mainly generated, while cytosolic TrxR plays a role to maintain optimal oxido-reductive status in cytosol. In this study, we report differential physiological functions of these two TrxRs in C. elegans. trxr-1, the cytosolic TrxR, is highly expressed in pharynx, vulva and intestine, whereas trxr-2, the mitochondrial TrxR, is mainly expressed in pharyngeal and body wall muscles. Deficiency of the non-selenoprotein trxr-2 caused defects in longevity and delayed development under stress conditions, while deletion mutation of the selenoprotein trxr-1 resulted in interference in acidification of lysosomal compartment in intestine. Interestingly, the acidification defect of trxr-1(jh143) deletion mutant was rescued, not only by selenocystein-containing wild type TRXR-1, but also cysteine-substituted mutant TRXR-1. Both trxr-1 and trxr-2 were up-regulated when worms were challenged by environmental stress such as heat shock. These results suggest that trxr-1 and trxr-2 function differently at organismal level presumably by their differential sub-cellular localization in C. elegans.

Keywords: C. elegans, longevity, oxidative stress, thioredoxin reductase, V-ATPase

Mol. Cells
Nov 30, 2022 Vol.45 No.11, pp. 763~867
COVER PICTURE
Naive (cyan) and axotomized (magenta) retinal ganglion cell axons in Xenopus tropicalis (Choi et al., pp. 846-854).

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