Abstract
The proteomics strategy was utilized to analyze and identify the gold adsorption proteins from Tepidimonas fonticaldi AT-A2, due to its outstanding performance in gold-binding and recovery. The results showed that three small proteins, including histidine biosynthesis protein (HisIE), iron donor protein (CyaY) and hypothetical protein_65aa, have a higher ability to adsorb gold ions because of the negatively charged domains or metal binding sites. On the other hand, the Salmonella PmrA/PmrB two-component system first replaces the iron (III)-binding motif using the peptide sequence from hypothetical protein_65aa, and this is then used to reveal the sensing and responsiveness to gold metal ions, which is totally different from the performance of traditional gold binding peptide (GBP) on the crystals on the surface of gold (111). We have successfully demonstrated an integrative proteomics and bacterial two-component system to explore the novel GBP. Finally, the heterologous over-expression of GBP by E. coli and the equilibrium of binding capacity for Au(III) have been conducted.
| Original language | English |
|---|---|
| Article number | 127 |
| Journal | Frontiers in Chemistry |
| Volume | 5 |
| Issue number | DEC |
| DOIs | |
| Publication status | Published - 2017 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
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Identification of gold sensing peptide by integrative proteomics and a bacterial two-component system. / Ng, I. Son; Yu, You Jin; Yi, Ying Chen; Tan, Shih I.; Huang, Bo Chuan; Han, Yin Lung.
In: Frontiers in Chemistry, Vol. 5, No. DEC, 127, 01.01.2017.Research output: Contribution to journal › Article
TY - JOUR
T1 - Identification of gold sensing peptide by integrative proteomics and a bacterial two-component system
AU - Ng, I. Son
AU - Yu, You Jin
AU - Yi, Ying Chen
AU - Tan, Shih I.
AU - Huang, Bo Chuan
AU - Han, Yin Lung
PY - 2017/1/1
Y1 - 2017/1/1
N2 - The proteomics strategy was utilized to analyze and identify the gold adsorption proteins from Tepidimonas fonticaldi AT-A2, due to its outstanding performance in gold-binding and recovery. The results showed that three small proteins, including histidine biosynthesis protein (HisIE), iron donor protein (CyaY) and hypothetical protein_65aa, have a higher ability to adsorb gold ions because of the negatively charged domains or metal binding sites. On the other hand, the Salmonella PmrA/PmrB two-component system first replaces the iron (III)-binding motif using the peptide sequence from hypothetical protein_65aa, and this is then used to reveal the sensing and responsiveness to gold metal ions, which is totally different from the performance of traditional gold binding peptide (GBP) on the crystals on the surface of gold (111). We have successfully demonstrated an integrative proteomics and bacterial two-component system to explore the novel GBP. Finally, the heterologous over-expression of GBP by E. coli and the equilibrium of binding capacity for Au(III) have been conducted.
AB - The proteomics strategy was utilized to analyze and identify the gold adsorption proteins from Tepidimonas fonticaldi AT-A2, due to its outstanding performance in gold-binding and recovery. The results showed that three small proteins, including histidine biosynthesis protein (HisIE), iron donor protein (CyaY) and hypothetical protein_65aa, have a higher ability to adsorb gold ions because of the negatively charged domains or metal binding sites. On the other hand, the Salmonella PmrA/PmrB two-component system first replaces the iron (III)-binding motif using the peptide sequence from hypothetical protein_65aa, and this is then used to reveal the sensing and responsiveness to gold metal ions, which is totally different from the performance of traditional gold binding peptide (GBP) on the crystals on the surface of gold (111). We have successfully demonstrated an integrative proteomics and bacterial two-component system to explore the novel GBP. Finally, the heterologous over-expression of GBP by E. coli and the equilibrium of binding capacity for Au(III) have been conducted.
UR - http://www.scopus.com/inward/record.url?scp=85041646412&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85041646412&partnerID=8YFLogxK
U2 - 10.3389/fchem.2017.00127
DO - 10.3389/fchem.2017.00127
M3 - Article
AN - SCOPUS:85041646412
VL - 5
JO - Frontiers in Chemistry
JF - Frontiers in Chemistry
SN - 2296-2646
IS - DEC
M1 - 127
ER -