Thiol-Rich Proteins Play Important Role in Adhesion and Sulfur Oxidation Process of Acidithiobacillus ferroxidans

Abstract:

The proteomics of the extracellular proteins (EPs), outer membrane proteins (OMPs) and the periplasmic proteins (PPs) of Acidithiobacillus ferrooxidans ATCC 23270 grown on Fe²⁺ and S⁰ substrates, respectively, were comparatively studied. 39 expression up-regulated proteins (including 13 EPs, 9 OMPs and 17 PPs) were identified and 70% of them contain cysteine residues in sequence. Some of the selected proteins especially the EPs contain abundant of the cysteine residues and one or more-CXXC-functional motifs. The thiol groups on the At. ferrooxidans cell surface were selectively marked by Ca²⁺ and SR-μ-XRF mapping in situ observation revealed that the number of thiols on the surface of the cells grown on S⁰ was about five times as that grown on Fe²⁺ substrate. When 0.01 g/L surfactant Tween-80 was added in the S⁰ culture medium, the adsorption and activation related EPs were down-regulated and the sulfur metabolism related proteins was up-regulated. The same phenomenon was observed when the cells were grown on the more easily adhesion sulfur allotrope μ-S. It indicates that the thiol-rich proteins played important roles in adhesion and sulfur oxidation process of At. ferrooxidans.

• Periodical: Advanced Materials Research (Volume 825)
• Pages: 137-140
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.825.137
• Online since: October 2013
• Authors: An An Peng, Jin Lan Xia, Hong Chang Liu, Wei Zhu, Rui Yong Zhang, Cheng Gui Zhang, Zhen Yuan Nie
• Keywords: Acidithiobacillus ferrooxidans, Differential Expression, Proteomics, Synchrotron Radiation, Thiol

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