Development of Bacterium-Based Heavy Metal Biosorbents: Enhanced Uptake of Cadmium and Mercury by Escherichia coli Expressing a Metal Binding Motif

1998 ◽  
Vol 64 (10) ◽  
pp. 4068-4072 ◽  
Author(s):  
Mehran Pazirandeh ◽  
Bridget M. Wells ◽  
Rebecca L. Ryan
Keyword(s):  
Escherichia Coli ◽  
Metal Binding ◽  
De Novo ◽  
Genetically Engineered ◽  
Peptide Sequence ◽  
Binding Motif ◽  
Bacterial Cells ◽  
Binding Peptide ◽  
Genetically Engineered Bacteria ◽  
Metal Binding Motif

ABSTRACT A gene coding for a de novo peptide sequence containing a metal binding motif was chemically synthesized and expressed inEscherichia coli as a fusion with the maltose binding protein. Bacterial cells expressing the metal binding peptide fusion demonstrated enhanced binding of Cd2+ and Hg2+compared to bacterial cells lacking the metal binding peptide. The potential use of genetically engineered bacteria as biosorbents for the removal of heavy metals from wastewaters is discussed.

scholarly journals Metal Binding Motif in the Active Site of the HDV Ribozyme Binds Divalent and Monovalent Ions

Biochemistry ◽  
2011 ◽  
Vol 50 (13) ◽  
pp. 2672-2682 ◽  
Author(s):  
Narayanan Veeraraghavan ◽  
Abir Ganguly ◽  
Jui-Hui Chen ◽  
Philip C. Bevilacqua ◽  
Sharon Hammes-Schiffer ◽  
...  
Keyword(s):  
Active Site ◽  
Metal Binding ◽  
Binding Motif ◽  
Monovalent Ions ◽  
Hdv Ribozyme ◽  
Metal Binding Motif

scholarly journals Metal ion recognition of the metal-binding motif in hammerhead ribozymes

2003 ◽  
Vol 43 (supplement) ◽  
pp. S28
Author(s):  
Y. Tanaka ◽  
Y. Kasai ◽  
C. Kojima ◽  
K. Yamasaki ◽  
H. Morita ◽  
...  
Keyword(s):  
Metal Binding ◽  
Metal Ion ◽  
Binding Motif ◽  
Hammerhead Ribozymes ◽  
Ion Recognition ◽  
Metal Binding Motif

Manganese and cobalt recovery by surface display of metal binding peptide on various loops of OmpC in Escherichia coli

2017 ◽  
Vol 45 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Murali kannan Maruthamuthu ◽  
Vidhya Selvamani ◽  
Saravanan Prabhu Nadarajan ◽  
Hyungdon Yun ◽  
You-Kwan Oh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Metal Binding ◽  
Surface Display ◽  
Binding Peptide ◽  
Cobalt Recovery

scholarly journals Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization

2004 ◽  
Vol 166 (7) ◽  
pp. 1003-1014 ◽  
Author(s):  
Gideon Lansbergen ◽  
Yulia Komarova ◽  
Mauro Modesti ◽  
Claire Wyman ◽  
Casper C. Hoogenraad ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Metal Binding ◽  
Intramolecular Interaction ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Scanning Force Microscopy ◽  
Binding Motif ◽  
Force Microscopy ◽  
Scanning Force ◽  
Metal Binding Motif

Cytoplasmic linker protein (CLIP)-170, CLIP-115, and the dynactin subunit p150Glued are structurally related proteins, which associate specifically with the ends of growing microtubules (MTs). Here, we show that down-regulation of CLIP-170 by RNA interference results in a strongly reduced accumulation of dynactin at the MT tips. The NH2 terminus of p150Glued binds directly to the COOH terminus of CLIP-170 through its second metal-binding motif. p150Glued and LIS1, a dynein-associating protein, compete for the interaction with the CLIP-170 COOH terminus, suggesting that LIS1 can act to release dynactin from the MT tips. We also show that the NH2-terminal part of CLIP-170 itself associates with the CLIP-170 COOH terminus through its first metal-binding motif. By using scanning force microscopy and fluorescence resonance energy transfer-based experiments we provide evidence for an intramolecular interaction between the NH2 and COOH termini of CLIP-170. This interaction interferes with the binding of the CLIP-170 to MTs. We propose that conformational changes in CLIP-170 are important for binding to dynactin, LIS1, and the MT tips.

The metal-binding motif of dipeptidyl peptidase III directly influences the enzyme activity in the copper derivative of dipeptidyl peptidase III

2004 ◽  
Vol 431 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Junzo Hirose ◽  
Hiroshi Kamigakiuchi ◽  
Hiroyuki Iwamoto ◽  
Hideaki Fujii ◽  
Masanori Nakai ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Metal Binding ◽  
Dipeptidyl Peptidase ◽  
Binding Motif ◽  
Metal Binding Motif

scholarly journals Interaction between a metal-binding motif of Hammerhead Ribozyme and divalent cations

2000 ◽  
Vol 40 (supplement) ◽  
pp. S94
Author(s):  
Y. Tanaka ◽  
E.H. Morita ◽  
H. Hayashi ◽  
Y. Kasa ◽  
T. Tanaka ◽  
...  
Keyword(s):  
Metal Binding ◽  
Divalent Cations ◽  
Hammerhead Ribozyme ◽  
Binding Motif ◽  
Metal Binding Motif
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