New amphiphilic neamine conjugates bearing a metal binding motif active against MDR E. aerogenes Gram-negative bacteria

2017 ◽  
Vol 127 ◽  
pp. 748-756 ◽  
Author(s):  
Anas Allam ◽  
Laure Maigre ◽  
Rodolphe Alves de Sousa ◽  
Estelle Dumont ◽  
Julia Vergalli ◽  
...  
Keyword(s):  
Metal Binding ◽  
Binding Motif ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Metal Binding Motif

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

Metal binding by Pseudomonas aeruginosa PAO1 is influenced by growth of the cells as a biofilm

1999 ◽  
Vol 45 (7) ◽  
pp. 616-622 ◽  
Author(s):  
S Langley ◽  
T J Beveridge
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Metal Binding ◽  
Gram Negative Bacteria ◽  
Binding Properties ◽  
Gram Negative ◽  
Pseudomonas Aeruginosa Pao1

The metal-binding properties of Pseudomonas aeruginosa PAO1 biofilms were investigated using four metals (Cu, Fe, Au, and La). All but one of the metals (i.e., Cu) were bound by the biofilms in amounts that were significantly greater than those bound by planktonically grown cells of the same strain. Lanthanum precipitation appeared to be limited to the base of the biofilms and was not promoted by a shift in lipopolysaccharide production by the cells.Key words: metal binding, biofilms, Gram-negative bacteria, bioremediation.

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

scholarly journals Identification of Methyl Halide-Utilizing Genes in the Methyl Bromide-Utilizing Bacterial Strain IMB-1 Suggests a High Degree of Conservation of Methyl Halide-Specific Genes in Gram-Negative Bacteria

2001 ◽  
Vol 67 (4) ◽  
pp. 1959-1963 ◽  
Author(s):  
Claire A. Woodall ◽  
Karen L. Warner ◽  
Ronald S. Oremland ◽  
J. Colin Murrell ◽  
Ian R. McDonald
Keyword(s):  
Energy Source ◽  
Methyl Bromide ◽  
Open Reading Frames ◽  
Binding Motif ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
High Sequence Homology ◽  
Methyl Halide ◽  
High Degree ◽  
Reading Frames

ABSTRACT Strain IMB-1, an aerobic methylotrophic member of the alpha subgroup of the Proteobacteria, can grow with methyl bromide as a sole carbon and energy source. A single cmugene cluster was identified in IMB-1 that contained six open reading frames: cmuC, cmuA, orf146, paaE, hutI, and partialmetF. CmuA from IMB-1 has high sequence homology to the methyltransferase CmuA from Methylobacterium chloromethanicum and Hyphomicrobium chloromethanicum and contains a C-terminal corrinoid-binding motif and an N-terminal methyltransferase motif. However,cmuB, identified in M. chloromethanicumand H. chloromethanicum, was not detected in IMB-1.

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