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

Published online July 25, 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
Feb 28, 2023 Vol.46 No.2, pp. 69~129
COVER PICTURE
The bulk tissue is a heterogeneous mixture of various cell types, which is depicted as a skein of intertwined threads with diverse colors each of which represents a unique cell type. Single-cell omics analysis untangles efficiently the skein according to the color by providing information of molecules at individual cells and interpretation of such information based on different cell types. The molecules that can be profiled at the individual cell by single-cell omics analysis includes DNA (bottom middle), RNA (bottom right), and protein (bottom left). This special issue reviews single-cell technologies and computational methods that have been developed for the single-cell omics analysis and how they have been applied to improve our understanding of the underlying mechanisms of biological and pathological phenomena at the single-cell level.

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