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Proteomic Insights into Sulfur Metabolism in the Hydrogen-Producing Hyperthermophilic Archaeon Thermococcus onnurineus NA1.

Authors :
Yoon-Jung Moon
Kwon, Joseph
Sung-Ho Yun
Hye Li Lim
Jonghyun Kim
Soo Jung Kim
Sung Gyun Kang
Jung-Hyun Lee
Seung Il Kim
Young-Ho Chung
Source :
International Journal of Molecular Sciences. 2015, Vol. 16 Issue 5, p9167-9195. 29p. 2 Diagrams, 3 Charts.
Publication Year :
2015

Abstract

The hyperthermophilic archaeon Thermococcus onnurineus NA1 has been shown to produce H² when using CO, formate, or starch as a growth substrate. This strain can also utilize elemental sulfur as a terminal electron acceptor for heterotrophic growth. To gain insight into sulfur metabolism, the proteome of T. onnurineus NA1 cells grown under sulfur culture conditions was quantified and compared with those grown under H²-evolving substrate culture conditions. Using label-free nano-UPLC-MSE-based comparative proteomic analysis, approximately 38.4% of the total identified proteome (589 proteins) was found to be significantly up-regulated (=1.5-fold) under sulfur culture conditions. Many of these proteins were functionally associated with carbon fixation, Fe-S cluster biogenesis, ATP synthesis, sulfur reduction, protein glycosylation, protein translocation, and formate oxidation. Based on the abundances of the identified proteins in this and other genomic studies, the pathways associated with reductive sulfur metabolism, H²-metabolism, and oxidative stress defense were proposed. The results also revealed markedly lower expression levels of enzymes involved in the sulfur assimilation pathway, as well as cysteine desulfurase, under sulfur culture condition. The present results provide the first global atlas of proteome changes triggered by sulfur, and may facilitate an understanding of how hyperthermophilic archaea adapt to sulfur-rich, extreme environments. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
16616596
Volume :
16
Issue :
5
Database :
Academic Search Index
Journal :
International Journal of Molecular Sciences
Publication Type :
Academic Journal
Accession number :
102922069
Full Text :
https://doi.org/10.3390/ijms16059167