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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
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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