CaltechAUTHORS
  A Caltech Library Service

The pio Operon Is Essential for Phototrophic Fe(II) Oxidation in Rhodopseudomonas palustris TIE-1

Jiao, Yongqin and Newman, Dianne K. (2007) The pio Operon Is Essential for Phototrophic Fe(II) Oxidation in Rhodopseudomonas palustris TIE-1. Journal of Bacteriology, 189 (5). pp. 1765-1773. ISSN 0021-9193. http://resolver.caltech.edu/CaltechAUTHORS:JIAjbact07

[img]
Preview
PDF
See Usage Policy.

272Kb

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:JIAjbact07

Abstract

Phototrophic Fe(II)-oxidizing bacteria couple the oxidation of ferrous iron [Fe(II)] to reductive CO2 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.


Item Type:Article
ORCID:
AuthorORCID
Newman, Dianne K.0000-0003-1647-1918
Additional Information:Copyright © 2007, American Society for Microbiology. Received 30 May 2006/ Accepted 12 December 2006. Published ahead of print on 22 December 2006. We give special thanks to C. Romano and S. Potter for help in sequencing pioA and pioB. We thank D. Lies and L. Dietrich for guidance throughout this study; D. Lies, N. Caizza, and C. Romano for comments on the manuscript; and all the Newman lab members for helpful discussions. This work was supported by grants from the Packard Foundation and the Howard Hughes Medical Institute to D.K.N.
Record Number:CaltechAUTHORS:JIAjbact07
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:JIAjbact07
Alternative URL:http://dx.doi.org/10.1128/JB.00776-06
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:7559
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:03 Mar 2007
Last Modified:24 Oct 2017 15:05

Repository Staff Only: item control page