English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The ABCB7-Like Transporter PexA in Rhodobacter capsulatus Is Involved in the Translocation of Reactive Sulfur Species

Riedel, S., Siemiatkowska, B., Watanabe, M., Müller, C. S., Schünemann, V., Hoefgen, R., et al. (2019). The ABCB7-Like Transporter PexA in Rhodobacter capsulatus Is Involved in the Translocation of Reactive Sulfur Species. Frontiers in Microbiology, 10: 406. doi:10.3389/fmicb.2019.00406.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0003-328C-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-328D-6
Genre: Journal Article

Files

show Files

Locators

show
hide
Locator:
Link (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Riedel, Simona1, Author
Siemiatkowska, B.2, Author              
Watanabe, M.3, Author              
Müller, Christina S.1, Author
Schünemann, Volker1, Author
Hoefgen, R.3, Author              
Leimkühler, Silke1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Regulation of Photosynthesis, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2205653              
3Amino Acid and Sulfur Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753337              

Content

show
hide
Free keywords: -
 Abstract: The mitochondrial ATP-binding cassette (ABC) transporters ABCB7 in humans, Atm1 in yeast and ATM3 in plants are highly conserved in their overall architecture and particularly in their glutathione binding pocket located within the transmembrane spanning domains. These transporters have attracted interest in the last two decades based on their proposed role in connecting the mitochondrial iron-sulfur (Fe-S) cluster assembly with its cytosolic Fe-S cluster assembly (CIA) counterpart. So far, the specific compound that is transported across the membrane remains unknown. In this report we characterized the ABCB7-like transporter Rcc02305 in Rhodobacter capsulatus, which shares 47 amino acid sequence identity to its mitochondrial counterpart. The constructed interposon mutant strain in R. capsulatus displayed increased levels of intracellular reactive oxygen species without a simultaneous accumulation of the cellular iron levels. The inhibition of endogenous glutathione biosynthesis resulted in an increase of total glutathione levels in the mutant strain. Bioinformatic analysis of the amino acid sequence motifs revealed a potential aminotransferase class-V pyridoxal-5’-phosphate (PLP) binding site that overlaps with the Walker A motif within the nucleotide binding domains of the transporter. PLP is a well characterized cofactor of L-cysteine desulfurases like IscS and NFS1 which has a role in the formation of a protein-bound persulfide group within these proteins. We therefore suggest to rename the ABCB7-like transporter Rcc02305 in R. capsulatus to PexA for PLP binding exporter. We further suggest that this ABC-transporter in R. capsulatus is involved in the formation and export of polysulfide species to the periplasm.

Details

show
hide
Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.3389/fmicb.2019.00406
BibTex Citekey: 10.3389/fmicb.2019.00406
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Frontiers in Microbiology
  Abbreviation : Front. Microbiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Lausanne : Frontiers Media
Pages: - Volume / Issue: 10 Sequence Number: 406 Start / End Page: - Identifier: ISSN: 1664-302X
CoNE: https://pure.mpg.de/cone/journals/resource/1664-302X