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pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8
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| Zeitschriftentitel: | Protein Science |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Protein Science, 15, 2006, 2, S. 335-342 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Mohan, P.M. Krishna Barve, Maneesha Chatterjee, Amarnath Hosur, Ramakrishna V. Mohan, P.M. Krishna Barve, Maneesha Chatterjee, Amarnath Hosur, Ramakrishna V. |
|---|---|
| author |
Mohan, P.M. Krishna Barve, Maneesha Chatterjee, Amarnath Hosur, Ramakrishna V. |
| spellingShingle |
Mohan, P.M. Krishna Barve, Maneesha Chatterjee, Amarnath Hosur, Ramakrishna V. Protein Science pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 Molecular Biology Biochemistry |
| author_sort |
mohan, p.m. krishna |
| spelling |
Mohan, P.M. Krishna Barve, Maneesha Chatterjee, Amarnath Hosur, Ramakrishna V. 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.051854906 <jats:title>Abstract</jats:title><jats:p>Dynein light chain protein, a part of the cytoplasmic motor assembly, is a homodimer at physiological pH and dissociates below pH 4.5 to a monomer. The dimer binds to a variety of cargo, whereas the monomer does not bind any of the target proteins. We report here the pH induced stepwise structural and motional changes in the protein, as derived from line broadening and <jats:sup>15</jats:sup>N transverse relaxation measurements. At pH 7 and below until 5, partial protonation and consequent interconversion between molecules carrying protonated and neutral histidines, causes conformational dynamics in the dimeric protein and this increases with decreasing pH. Enhanced dynamics in turn leads to partial loosening of the structure. This would have implications for different efficacies of binding by target proteins due to small variations in pH in different parts of the cell, and hence for cargo trafficking from one part to another. Below pH 5, enhanced charge repulsions, partial loss of hydrophobic interactions, and destabilization of H‐bonds across the dimer interface cause further loosening of the dimeric structure, leading eventually to the dissociation of the dimer.</jats:p> pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 Protein Science |
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| title |
pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_unstemmed |
pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_full |
pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_fullStr |
pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_full_unstemmed |
pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_short |
pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_sort |
ph driven conformational dynamics and dimer‐to‐monomer transition in dlc8 |
| topic |
Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1110/ps.051854906 |
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2006 |
| physical |
335-342 |
| description |
<jats:title>Abstract</jats:title><jats:p>Dynein light chain protein, a part of the cytoplasmic motor assembly, is a homodimer at physiological pH and dissociates below pH 4.5 to a monomer. The dimer binds to a variety of cargo, whereas the monomer does not bind any of the target proteins. We report here the pH induced stepwise structural and motional changes in the protein, as derived from line broadening and <jats:sup>15</jats:sup>N transverse relaxation measurements. At pH 7 and below until 5, partial protonation and consequent interconversion between molecules carrying protonated and neutral histidines, causes conformational dynamics in the dimeric protein and this increases with decreasing pH. Enhanced dynamics in turn leads to partial loosening of the structure. This would have implications for different efficacies of binding by target proteins due to small variations in pH in different parts of the cell, and hence for cargo trafficking from one part to another. Below pH 5, enhanced charge repulsions, partial loss of hydrophobic interactions, and destabilization of H‐bonds across the dimer interface cause further loosening of the dimeric structure, leading eventually to the dissociation of the dimer.</jats:p> |
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| author | Mohan, P.M. Krishna, Barve, Maneesha, Chatterjee, Amarnath, Hosur, Ramakrishna V. |
| author_facet | Mohan, P.M. Krishna, Barve, Maneesha, Chatterjee, Amarnath, Hosur, Ramakrishna V., Mohan, P.M. Krishna, Barve, Maneesha, Chatterjee, Amarnath, Hosur, Ramakrishna V. |
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| description | <jats:title>Abstract</jats:title><jats:p>Dynein light chain protein, a part of the cytoplasmic motor assembly, is a homodimer at physiological pH and dissociates below pH 4.5 to a monomer. The dimer binds to a variety of cargo, whereas the monomer does not bind any of the target proteins. We report here the pH induced stepwise structural and motional changes in the protein, as derived from line broadening and <jats:sup>15</jats:sup>N transverse relaxation measurements. At pH 7 and below until 5, partial protonation and consequent interconversion between molecules carrying protonated and neutral histidines, causes conformational dynamics in the dimeric protein and this increases with decreasing pH. Enhanced dynamics in turn leads to partial loosening of the structure. This would have implications for different efficacies of binding by target proteins due to small variations in pH in different parts of the cell, and hence for cargo trafficking from one part to another. Below pH 5, enhanced charge repulsions, partial loss of hydrophobic interactions, and destabilization of H‐bonds across the dimer interface cause further loosening of the dimeric structure, leading eventually to the dissociation of the dimer.</jats:p> |
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| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
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| spelling | Mohan, P.M. Krishna Barve, Maneesha Chatterjee, Amarnath Hosur, Ramakrishna V. 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.051854906 <jats:title>Abstract</jats:title><jats:p>Dynein light chain protein, a part of the cytoplasmic motor assembly, is a homodimer at physiological pH and dissociates below pH 4.5 to a monomer. The dimer binds to a variety of cargo, whereas the monomer does not bind any of the target proteins. We report here the pH induced stepwise structural and motional changes in the protein, as derived from line broadening and <jats:sup>15</jats:sup>N transverse relaxation measurements. At pH 7 and below until 5, partial protonation and consequent interconversion between molecules carrying protonated and neutral histidines, causes conformational dynamics in the dimeric protein and this increases with decreasing pH. Enhanced dynamics in turn leads to partial loosening of the structure. This would have implications for different efficacies of binding by target proteins due to small variations in pH in different parts of the cell, and hence for cargo trafficking from one part to another. Below pH 5, enhanced charge repulsions, partial loss of hydrophobic interactions, and destabilization of H‐bonds across the dimer interface cause further loosening of the dimeric structure, leading eventually to the dissociation of the dimer.</jats:p> pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 Protein Science |
| spellingShingle | Mohan, P.M. Krishna, Barve, Maneesha, Chatterjee, Amarnath, Hosur, Ramakrishna V., Protein Science, pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8, Molecular Biology, Biochemistry |
| title | pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_full | pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_fullStr | pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_full_unstemmed | pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_short | pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| title_sort | ph driven conformational dynamics and dimer‐to‐monomer transition in dlc8 |
| title_unstemmed | pH driven conformational dynamics and dimer‐to‐monomer transition in DLC8 |
| topic | Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1110/ps.051854906 |