English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability

Missirlis, F., Ulschmid, J. K., Hirosawa-Takamori, M., Groenke, S., Schaefer, U., Becker, K., et al. (2002). Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability. Journal of Biological Chemistry, 277(13), 11521-11526. Retrieved from http://www.jbc.org/content/277/13/11521.full.pdf+html.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F40D-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E0D8-2
Genre: Journal Article

Files

show Files
hide Files
:
599664.pdf (Publisher version), 732KB
Name:
599664.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Missirlis, F.1, Author              
Ulschmid, J. K., Author
Hirosawa-Takamori, M., Author
Groenke, S.1, Author              
Schaefer, U.1, Author              
Becker, K., Author
Phillips, J. P., Author
Jaeckle, H.1, Author              
Affiliations:
1Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society, ou_578590              

Content

show
hide
Free keywords: -
 Abstract: Defense against oxidative stress in mammals includes the regeneration of the major thiol reductants glutathione and thioredoxin by glutathione reductase and thioredoxin reductase (TrxR), respectively. In contrast, Drosophila, and possibly insects in general, lacks glutathione reductase and must rely solely on the TrxR system. The mammalian TrxRs described so far are selenoproteins that utilize NADPH to reduce protein as well as nonprotein substrates in mitochondria and cytoplasm of cells. We show that a single Drosophila gene, Trxr-1, encodes non-selenocysteine-containing cytoplasmic and mitochondrial TrxR isoforms that differ with respect to their N termini. We generated transcript-specific mutants and used in vivo approaches to explore the biological functions of the two enzyme variants by introducing the corresponding transgenes into different Trxr-1 mutants. The results show that, although the two TrxR isoforms have similar biochemical properties, their biological functions are not interchangeable.

Details

show
hide
Language(s):
 Dates: 2002-03-29
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biological Chemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 277 (13) Sequence Number: - Start / End Page: 11521 - 11526 Identifier: -