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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Gloeckner Foundation 3xflagtwin strep affinity tag-based tandem affinity purification method
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
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Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the Ni-NTA-derivatized sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.

Journal: The Journal of Biological Chemistry

Article Title: The DNA-binding protein HU is a molecular glue that attaches bacteria to extracellular DNA in biofilms

doi: 10.1016/j.jbc.2021.100532

Figure Lengend Snippet: Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the Ni-NTA-derivatized sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.

Article Snippet: Proteins were purified using standard Ni-NTA affinity-purification IMAC methods (Qiagen QIAexpressionist) under nondenaturing conditions.

Techniques: Binding Assay, Microscale Thermophoresis, Concentration Assay, Fluorescence, Diffusion-based Assay, Spectroscopy, SDS Page