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Title: 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.

Authors:
; ; ; ; ; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
981994
Report Number(s):
PNNL-SA-52140
Journal ID: ISSN 1040-0397; ISSN 1521-4109; TRN: US201012%%1430
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Journal Name:
Electroanalysis, 22(7-8):856-864
Additional Journal Information:
Journal Volume: 22; Journal Issue: 7-8; Journal ID: ISSN 1040-0397
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; BINDING ENERGY; CHROMIUM; DMSO; ELECTRON TRANSFER; ELECTRONS; FUNCTIONS; GENES; GROWTH; METALS; MUTANTS; OXIDES; PROCESSING; PROTEINS; REDUCTION; RESPIRATION; SECRETION; SURFACES; TRANSPOSONS; URANIUM; VALENCE

Citation Formats

Bouhenni, Rachida, Vora, Gary J, Biffinger, Justin C, Shirodkar, Sheetal, Brockman, K L, Ray, Ricky, Wu, Peter, Johnson, Brandy J, Biddle, E M, Marshall, Matthew J, Fitzgerald, Lisa A, Little, Brenda, Fredrickson, Jim K, Beliaev, Alex S, Ringeisen, Bradley R, and Saffarini, Daad. The role of Shewanella oneidensis MR-1 outer surface structures in extracellular electron transfer. United States: N. p., 2010. Web. doi:10.1002/elan.200880006.
Bouhenni, Rachida, Vora, Gary J, Biffinger, Justin C, Shirodkar, Sheetal, Brockman, K L, Ray, Ricky, Wu, Peter, Johnson, Brandy J, Biddle, E M, Marshall, Matthew J, Fitzgerald, Lisa A, Little, Brenda, Fredrickson, Jim K, Beliaev, Alex S, Ringeisen, Bradley R, & Saffarini, Daad. The role of Shewanella oneidensis MR-1 outer surface structures in extracellular electron transfer. United States. https://doi.org/10.1002/elan.200880006
Bouhenni, Rachida, Vora, Gary J, Biffinger, Justin C, Shirodkar, Sheetal, Brockman, K L, Ray, Ricky, Wu, Peter, Johnson, Brandy J, Biddle, E M, Marshall, Matthew J, Fitzgerald, Lisa A, Little, Brenda, Fredrickson, Jim K, Beliaev, Alex S, Ringeisen, Bradley R, and Saffarini, Daad. 2010. "The role of Shewanella oneidensis MR-1 outer surface structures in extracellular electron transfer". United States. https://doi.org/10.1002/elan.200880006.
@article{osti_981994,
title = {The role of Shewanella oneidensis MR-1 outer surface structures in extracellular electron transfer},
author = {Bouhenni, Rachida and Vora, Gary J and Biffinger, Justin C and Shirodkar, Sheetal and Brockman, K L and Ray, Ricky and Wu, Peter and Johnson, Brandy J and Biddle, E M and Marshall, Matthew J and Fitzgerald, Lisa A and Little, Brenda and Fredrickson, Jim K and Beliaev, Alex S and Ringeisen, Bradley R and Saffarini, Daad},
abstractNote = {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.},
doi = {10.1002/elan.200880006},
url = {https://www.osti.gov/biblio/981994}, journal = {Electroanalysis, 22(7-8):856-864},
issn = {1040-0397},
number = 7-8,
volume = 22,
place = {United States},
year = {Tue Apr 20 00:00:00 EDT 2010},
month = {Tue Apr 20 00:00:00 EDT 2010}
}