Electron microscopic study of compaction of individual DNA molecules with histone H1 in surface films
Interaction of individual spread DNA molecules with histone H1 was studied by electron microscopy using the protein-free spreading technique. It was shown that in the presence of 0.2–5 μg/ml of histone H1 in hypophase there are three types of structures in electron-microscopic preparations: fibres o...
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Veröffentlicht in: | FEBS letters 1993-05, Vol.322 (3), p.311-314 |
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description | Interaction of individual spread DNA molecules with histone H1 was studied by electron microscopy using the protein-free spreading technique. It was shown that in the presence of 0.2–5 μg/ml of histone H1 in hypophase there are three types of structures in electron-microscopic preparations: fibres of non-compacted DNA, compact fibres with twisted strands of duplex DNA and compacted rod-like and circular structures where the separate fibres of duplex DNA could not be distinguished. The study of compact structure morphology allows us to conclude that they are formed by side-by-side association of DNA fibres. At an increase of ionic strength there is a tendency for transition from the second to the third type structures. The latter can be explained by transition from non-cooperative to cooperative binding of histone H1 to DNA. Regularities established for interaction between DNA and histone H1 can be useful for understanding the role of histone H1 in the higher order structure organization of chromatin. |
doi_str_mv | 10.1016/0014-5793(93)81593-O |
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It was shown that in the presence of 0.2–5 μg/ml of histone H1 in hypophase there are three types of structures in electron-microscopic preparations: fibres of non-compacted DNA, compact fibres with twisted strands of duplex DNA and compacted rod-like and circular structures where the separate fibres of duplex DNA could not be distinguished. The study of compact structure morphology allows us to conclude that they are formed by side-by-side association of DNA fibres. At an increase of ionic strength there is a tendency for transition from the second to the third type structures. The latter can be explained by transition from non-cooperative to cooperative binding of histone H1 to DNA. Regularities established for interaction between DNA and histone H1 can be useful for understanding the role of histone H1 in the higher order structure organization of chromatin.</description><subject>Animals</subject><subject>Cattle</subject><subject>Compaction</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - ultrastructure</subject><subject>Histone H1</subject><subject>Histones - chemistry</subject><subject>Histones - ultrastructure</subject><subject>Microscopy, Electron</subject><subject>Protein-free film method</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtr3DAUhUVpSSePf9CCVqVduJWsh61NIUlnmkLobJK1kKUromJbU8lOmH9fOTNkWQICce8590j6hNAHSr5SQuU3QiivRKPYZ8W-tFQoVm3foBVtG1YxLtu3aPVieY9Oc_5DSt1SdYJOWt5KKsUKwboHO6U44iHYFLONu2Bxnma3x9FjG4edsVMoeqnC6MJjcLPp8Y_fl3iIZXbuIeOnMD3gh5CnOAK-ocWI85y8sYB96Id8jt5502e4OO5n6H6zvru-qW63P39dX95Wlku5rToQrYOOuYYacMQL38m6A0lqSYTiqmGKCO6JM7Tuau-lg9Z7I5xrOu64Y2fo0yF3l-LfGfKkh5At9L0ZIc5ZN6KplWhIMfKDcXlzTuD1LoXBpL2mRC909YJOL-h0Wc909baMfTzmz90A7mXoiLPom4P-FHrYvypTb9ZX9SIsfcWeu8tB3w9BUGg9Bkg62wCjBRdS-S_tYvj_Tf8BLuGerg</recordid><startdate>19930517</startdate><enddate>19930517</enddate><creator>Vengerov, Yuri Yu</creator><creator>Martinkina, Larissa P.</creator><creator>Semenov, Timur E.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19930517</creationdate><title>Electron microscopic study of compaction of individual DNA molecules with histone H1 in surface films</title><author>Vengerov, Yuri Yu ; Martinkina, Larissa P. ; Semenov, Timur E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466O-be58deb3d71aed0f5fb62be602605949739054f0da12b2ff6de8ffa5dd7b4d4d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Compaction</topic><topic>DNA</topic><topic>DNA - chemistry</topic><topic>DNA - ultrastructure</topic><topic>Histone H1</topic><topic>Histones - chemistry</topic><topic>Histones - ultrastructure</topic><topic>Microscopy, Electron</topic><topic>Protein-free film method</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vengerov, Yuri Yu</creatorcontrib><creatorcontrib>Martinkina, Larissa P.</creatorcontrib><creatorcontrib>Semenov, Timur E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vengerov, Yuri Yu</au><au>Martinkina, Larissa P.</au><au>Semenov, Timur E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electron microscopic study of compaction of individual DNA molecules with histone H1 in surface films</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1993-05-17</date><risdate>1993</risdate><volume>322</volume><issue>3</issue><spage>311</spage><epage>314</epage><pages>311-314</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Interaction of individual spread DNA molecules with histone H1 was studied by electron microscopy using the protein-free spreading technique. It was shown that in the presence of 0.2–5 μg/ml of histone H1 in hypophase there are three types of structures in electron-microscopic preparations: fibres of non-compacted DNA, compact fibres with twisted strands of duplex DNA and compacted rod-like and circular structures where the separate fibres of duplex DNA could not be distinguished. The study of compact structure morphology allows us to conclude that they are formed by side-by-side association of DNA fibres. At an increase of ionic strength there is a tendency for transition from the second to the third type structures. The latter can be explained by transition from non-cooperative to cooperative binding of histone H1 to DNA. 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subjects | Animals Cattle Compaction DNA DNA - chemistry DNA - ultrastructure Histone H1 Histones - chemistry Histones - ultrastructure Microscopy, Electron Protein-free film method |
title | Electron microscopic study of compaction of individual DNA molecules with histone H1 in surface films |
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