NDLI: Cellular response of E. coli upon Hg<sup>2+</sup> exposure – a case study of advanced nuclear analytical approach to metalloproteomics

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Cellular response of E. coli upon Hg²⁺ exposure – a case study of advanced nuclear analytical approach to metalloproteomics

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Metallomics Vol - 5 Issue - 6

Metallomics Vol - 5 Issue - 5

Metallomics Vol - 5 Issue - 4

Metallomics Vol - 5 Issue - 3

Metallomics Vol - 5 Issue - 2

Cellular response of E. coli upon Hg²⁺ exposure – a case study of advanced nuclear analytical approach to metalloproteomics

Content Provider	Royal Society of Chemistry (RSC)
Author	Zhang, Jinchao Hu, Yi Gao, Yuxi Chai, Zhifang Zhao, Jiating Li, Bai Peng, Xiaomin Li, Yunyun Li, Yufeng
Copyright Year	2013
Abstract	The response of E. coli to Hg2+ exposure was investigated using proteomic and metalloproteomic approaches. E. coli was cultured in the LB medium containing HgCl2 and/or selenomethionine. The growth curve of E. coli was measured to estimate the toxicity of Hg2+ or selenomethionine. After two-dimensional gel electrophoresis (2-DE), distribution of Hg in 2-DE gel was detected with synchrotron radiation X-ray fluorescence (SRXRF) at 4W1B, Beijing Synchrotron Radiation Facility. The proteins with differential expression and those containing Hg were identified with electrospray ionization tandem mass spectrometry (ESI-MS/MS) and peptide mass fingerprinting analysis. The results showed that Hg2+ can inhibit the growth of E. coli, while supplement of selenomethionine can shorten the lag period induced by Hg2+, indicating an antagonistic effect of selenomethionine against Hg2+ toxicity. Mechanistically, Hg was observed to be able to bind pyruvate kinase, a glycolytic enzyme, and modulate the expression of five other proteins, including down-regulation of outer membrane protein W and up-regulation of transcription termination factor rho, cysteine synthase, transaldolase A and alkyl hydroperoxide reductase subunit C. Therefore, our results indicated that mercury may influence osmosis of plasma membrane, antioxidant defense, and glycometabolism of the microorganism. This study demonstrates the high sensitivity of SRXRF in identifying metal-associated proteins compared to conventional proteomic approaches.
Starting Page	913
Ending Page	919
Page Count	7
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	5
Issue Number	7
Journal	Metallomics
DOI	10.1039/c3mt20279h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Membrane protein Cell membrane Enzyme Escherichia coli Electrospray ionization coli Pyruvic acid Osmosis Antioxidant Beijing Peptide mass fingerprinting X-ray fluorescence Lysogeny broth Ionization Kinase Alkyl Cysteine synthase Two-dimensional gel electrophoresis Microorganism Synchrotron Mercury poisoning Mass spectrometry Organic peroxide Selenomethionine
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Cellular response of E. coli upon Hg²⁺ exposure – a case study of advanced nuclear analytical approach to metalloproteomics

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Cellular response of E. coli upon Hg2+ exposure – a case study of advanced nuclear analytical approach to metalloproteomics

Cellular response of E. coli upon Hg²⁺ exposure – a case study of advanced nuclear analytical approach to metalloproteomics