April 20, 2010
Journal Article

The role of Shewanella oneidensis MR-1 outer surface structures in extracellular electron transfer

Abstract

Shewanella oneidensis is a facultative anaerobe that uses more than 14 different terminal electron acceptors for respiration. These include metal oxides and hydroxyoxides, and toxic metals such as uranium and chromium. Mutants deficient in metal reduction were isolated using the mariner transposon derivative, minihimar RB1. These included mutants with transposon insertions in the prepilin peptidase and type II secretion system genes. All mutants were deficient in Fe(III) and Mn(IV) reduction, and exhibited slow growth when DMSO was used as the electron acceptor. The genome sequence of S. oneidensis contains one prepilin peptidase gene, pilD. A similar prepilin peptidase that may function in the processing of type II secretion prepilins was not found. Single and multiple chromosomal deletions of four putative type IV pilin genes did not affect Fe(III) and Mn(IV) reduction. These results indicate that PilD in S. oneidensis is responsible for processing both type IV and type II secretion prepilin proteins. Type IV pili do not appear to be required for Fe(III) and Mn(IV) reduction.

Revised: June 15, 2010 | Published: April 20, 2010

Citation

Bouhenni R., G.J. Vora, J.C. Biffinger, S. Shirodkar, K.L. Brockman, R. Ray, and P. Wu, et al. 2010. The role of Shewanella oneidensis MR-1 outer surface structures in extracellular electron transfer. Electroanalysis 22, no. 7-8:856-864. PNNL-SA-52140.