Pulling a Single Chromatin Fiber Reveals the Forces That Maintain Its Higher-Order Structure
Single chicken erythrocyte chromatin fibers were stretched and released at room temperature with force-measuring laser tweezers. In low ionic strength, the stretch-release curves reveal a process of continuous deformation with little or no internucleosomal attraction. A persistence length of 30 nm a...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-01, Vol.97 (1), p.127-132 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Cui, Yujia Bustamante, Carlos |
| description | Single chicken erythrocyte chromatin fibers were stretched and released at room temperature with force-measuring laser tweezers. In low ionic strength, the stretch-release curves reveal a process of continuous deformation with little or no internucleosomal attraction. A persistence length of 30 nm and a stretch modulus of ≈ 5 pN is determined for the fibers. At forces of 20 pN and higher, the fibers are modified irreversibly, probably through the mechanical removal of the histone cores from native chromatin. In 40-150 mM NaCl, a distinctive condensation-decondensation transition appears between 5 and 6 pN, corresponding to an internucleosomal attraction energy of ≈ 2.0 kcal/mol per nucleosome. Thus, in physiological ionic strength the fibers possess a dynamic structure in which the fiber locally interconverting between "open" and "closed" states because of thermal fluctuations. |
| doi_str_mv | 10.1073/pnas.97.1.127 |
| format | Article |
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In low ionic strength, the stretch-release curves reveal a process of continuous deformation with little or no internucleosomal attraction. A persistence length of 30 nm and a stretch modulus of ≈ 5 pN is determined for the fibers. At forces of 20 pN and higher, the fibers are modified irreversibly, probably through the mechanical removal of the histone cores from native chromatin. In 40-150 mM NaCl, a distinctive condensation-decondensation transition appears between 5 and 6 pN, corresponding to an internucleosomal attraction energy of ≈ 2.0 kcal/mol per nucleosome. 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In low ionic strength, the stretch-release curves reveal a process of continuous deformation with little or no internucleosomal attraction. A persistence length of 30 nm and a stretch modulus of ≈ 5 pN is determined for the fibers. At forces of 20 pN and higher, the fibers are modified irreversibly, probably through the mechanical removal of the histone cores from native chromatin. In 40-150 mM NaCl, a distinctive condensation-decondensation transition appears between 5 and 6 pN, corresponding to an internucleosomal attraction energy of ≈ 2.0 kcal/mol per nucleosome. Thus, in physiological ionic strength the fibers possess a dynamic structure in which the fiber locally interconverting between "open" and "closed" states because of thermal fluctuations.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10618382</pmid><doi>10.1073/pnas.97.1.127</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Biological Sciences Chickens Chromatin Chromatin - chemistry Curvature Deoxyribonucleic acid DNA Elastic tissue Elasticity Erythrocytes Erythrocytes - chemistry Histones Histones - chemistry Hysteresis Lasers Microscopy Nucleosomes Nucleosomes - chemistry Osmolar Concentration Physics Polystyrenes Sodium Chloride - pharmacology Stress, Mechanical Thermodynamics |
| title | Pulling a Single Chromatin Fiber Reveals the Forces That Maintain Its Higher-Order Structure |
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