Two thioredoxin reductases, trxr-1 and trxr-2, have differential physiological roles in Caenorhabditis elegans
- Authors
- Li, Weixun; Bandyopadhyay, Jaya; Hwaang, Hyun Sook; Park, Byung-Jae; Cho, Jeong Hoon; Il Lee, Jin; Ahnn, Joohong; Lee, Sun-Kyung
- Issue Date
- Aug-2012
- Publisher
- KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
- Keywords
- C. elegans; longevity; oxidative stress; thioredoxin reductase; V-ATPase
- Citation
- MOLECULES AND CELLS, v.34, no.2, pp.209 - 218
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- MOLECULES AND CELLS
- Volume
- 34
- Number
- 2
- Start Page
- 209
- End Page
- 218
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/164994
- DOI
- 10.1007/s10059-012-0155-6
- ISSN
- 1016-8478
- Abstract
- Thioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide reductase family, which mainly functions in the thioredoxin system. TrxR is found in all living organisms and exists in two major ubiquitous isoenzymes 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.
- Files in This Item
-
Go to Link
- Appears in
Collections - 서울 자연과학대학 > 서울 생명과학과 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.