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PMID: 17189359 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1.

Journal of bacteriology ·Vol. 189 ·No. 5 ·2007-03-00 ·Pages 1765-73

Jiao Y, Newman DK

Abstract

Phototrophic Fe(II)-oxidizing bacteria couple the oxidation of ferrous iron [Fe(II)] to reductive CO(2) fixation by using light energy, but until recently, little has been understood about the molecular basis for this process. Here we report the discovery, with Rhodopseudomonas palustris TIE-1 as a model organism, of a three-gene operon, designated the pio operon (for phototrophic iron oxidation), that is necessary for phototrophic Fe(II) oxidation. The first gene in the operon, pioA, encodes a c-type cytochrome that is upregulated under Fe(II)-grown conditions. PioA contains a signal sequence and shares homology with MtrA, a decaheme c-type cytochrome from Shewanella oneidensis MR-1. The second gene, pioB, encodes a putative outer membrane beta-barrel protein. PioB is a homologue of MtrB from S. oneidensis MR-1. The third gene, pioC, encodes a putative high potential iron sulfur protein (HiPIP) with a twin-arginine translocation (Tat) signal sequence and is similar to the putative Fe(II) oxidoreductase (Iro) from Acidithiobacillus ferrooxidans. Like PioA, PioB and PioC appear to be secreted proteins. Deletion of the pio operon results in loss of Fe(II) oxidation activity and growth on Fe(II). Complementation studies confirm that the phenotype of this mutant is due to loss of the pio genes. Deletion of pioA alone results in loss of almost all Fe(II) oxidation activity; however, deletion of either pioB or pioC alone results in only partial loss of Fe(II) oxidation activity. Together, these results suggest that proteins encoded by the pio operon are essential and specific for phototrophic Fe(II) oxidation in R. palustris TIE-1.

MeSH Terms
Base Sequence Cytochromes c/metabolism Iron/metabolism Molecular Sequence Data Operon Oxidation-Reduction Oxidoreductases/genetics Rhodopseudomonas/genetics,metabolism
Chemicals
Cytochromes c Iron Oxidoreductases high-potential iron-sulfur protein oxygen oxidoreductase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jiao Yongqin
Division of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125, USA.
Newman Dianne K
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.00776-06
Published
2007-03-00
Epub
2006-00-22
Pages
1765-73
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC1855732
Subset
IM
Databases
GENBANK
EF119739, EF119740, EF119741
External Links
PubMed source DOI: 10.1128/JB.00776-06 PMC Full Text View journal details
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