Electron microscopic study of the repressor of bacteriophage λ and its interaction with operator DNA
Identifieur interne : 000258 ( Istex/Corpus ); précédent : 000257; suivant : 000259Electron microscopic study of the repressor of bacteriophage λ and its interaction with operator DNA
Auteurs : Christine Brack ; Vincenzo PirrottaSource :
- Journal of Molecular Biology [ 0022-2836 ] ; 1973.
Abstract
The structure of purified phage λ repressor has been examined by high resolution electron microscopy. The repressor molecule appears predominantly as a tetramer of about 95 Å × 120 Å. We have proposed a model to account for the variety of aspects seen on the electron micrographs. Spreading DNA without protein film and use of uranyl formate staining allowed the simultaneous visualization of the DNA and the structure of the repressor molecule bound to it. Mapping the positions of λ repressor bound to whole λ DNA shows preferential binding to the region containing the operators. At high resolution multiple binding of repressor to the operator can be demonstrated. Depending on the amount of repressor present, rows of one to four repressor tetramers are seen on the DNA, confirming the model of the operator containing four binding sites for repressor. The bound repressor can consequently protect against nuclease digestion of operator pieces of approximately 30, 57, 87 and 111 base-pairs. The isolated operator appears in the electron microscope as short double-stranded DNA fragments which can be shown to rebind repressor.
Url:
DOI: 10.1016/0022-2836(75)90187-4
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The repressor molecule appears predominantly as a tetramer of about 95 Å × 120 Å. We have proposed a model to account for the variety of aspects seen on the electron micrographs. Spreading DNA without protein film and use of uranyl formate staining allowed the simultaneous visualization of the DNA and the structure of the repressor molecule bound to it. Mapping the positions of λ repressor bound to whole λ DNA shows preferential binding to the region containing the operators. At high resolution multiple binding of repressor to the operator can be demonstrated. Depending on the amount of repressor present, rows of one to four repressor tetramers are seen on the DNA, confirming the model of the operator containing four binding sites for repressor. The bound repressor can consequently protect against nuclease digestion of operator pieces of approximately 30, 57, 87 and 111 base-pairs. The isolated operator appears in the electron microscope as short double-stranded DNA fragments which can be shown to rebind repressor.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Christine Brack</name><affiliations><json:string>Department of Microbiology Biozentrum der Universität Basel Klingelbergstrasse 70 CH-4056 Basel, Switzerland</json:string></affiliations></json:item><json:item><name>Vincenzo Pirrotta</name><affiliations><json:string>Department of Microbiology Biozentrum der Universität Basel Klingelbergstrasse 70 CH-4056 Basel, Switzerland</json:string></affiliations></json:item></author><language><json:string>eng</json:string></language><abstract>The structure of purified phage λ repressor has been examined by high resolution electron microscopy. The repressor molecule appears predominantly as a tetramer of about 95 Å × 120 Å. We have proposed a model to account for the variety of aspects seen on the electron micrographs. Spreading DNA without protein film and use of uranyl formate staining allowed the simultaneous visualization of the DNA and the structure of the repressor molecule bound to it. Mapping the positions of λ repressor bound to whole λ DNA shows preferential binding to the region containing the operators. At high resolution multiple binding of repressor to the operator can be demonstrated. Depending on the amount of repressor present, rows of one to four repressor tetramers are seen on the DNA, confirming the model of the operator containing four binding sites for repressor. The bound repressor can consequently protect against nuclease digestion of operator pieces of approximately 30, 57, 87 and 111 base-pairs. The isolated operator appears in the electron microscope as short double-stranded DNA fragments which can be shown to rebind repressor.</abstract><qualityIndicators><score>7.148</score><pdfVersion>1.3</pdfVersion><pdfPageSize>468 x 684 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>1132</abstractCharCount><pdfWordCount>6391</pdfWordCount><pdfCharCount>38591</pdfCharCount><pdfPageCount>22</pdfPageCount><abstractWordCount>179</abstractWordCount></qualityIndicators><title>Electron microscopic study of the repressor of bacteriophage λ and its interaction with operator DNA</title><pii><json:string>0022-2836(75)90187-4</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>96</volume><pii><json:string>S0022-2836(00)X0746-2</json:string></pii><pages><last>144</last><first>139</first></pages><issn><json:string>0022-2836</json:string></issn><issue>1</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><title>Journal of Molecular Biology</title><publicationDate>1975</publicationDate></host><categories><wos><json:string>BIOCHEMISTRY & MOLECULAR BIOLOGY</json:string></wos></categories><publicationDate>1973</publicationDate><copyrightDate>1975</copyrightDate><doi><json:string>10.1016/0022-2836(75)90187-4</json:string></doi><id>EC56A33E04A2DA0423EBC63EBBD4E488C49BDC40</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/EC56A33E04A2DA0423EBC63EBBD4E488C49BDC40/fulltext/pdf</uri></json:item><json:item><original>true</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/EC56A33E04A2DA0423EBC63EBBD4E488C49BDC40/fulltext/txt</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/EC56A33E04A2DA0423EBC63EBBD4E488C49BDC40/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/EC56A33E04A2DA0423EBC63EBBD4E488C49BDC40/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Electron microscopic study of the repressor of bacteriophage λ and its interaction with operator DNA</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1975</date></publicationStmt><notesStmt><note>Some of the repressor and operator preparations used in this work were isolated during a stay at the Microbial Genetics Laboratory, Karolinska Institute, Stockholm, with the support of an EMBO Senior Research Fellowship and of a grant (B72-16X) from the Swedish Medical Research Council.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Electron microscopic study of the repressor of bacteriophage λ and its interaction with operator DNA</title><author><persName><forename type="first">Christine</forename><surname>Brack</surname></persName><affiliation>Department of Microbiology Biozentrum der Universität Basel Klingelbergstrasse 70 CH-4056 Basel, Switzerland</affiliation></author><author><persName><forename type="first">Vincenzo</forename><surname>Pirrotta</surname></persName><affiliation>Department of Microbiology Biozentrum der Universität Basel Klingelbergstrasse 70 CH-4056 Basel, Switzerland</affiliation></author></analytic><monogr><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="pISSN">0022-2836</idno><idno type="PII">S0022-2836(00)X0746-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1973"></date><biblScope unit="volume">96</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="139">139</biblScope><biblScope unit="page" to="144">144</biblScope></imprint></monogr><idno type="istex">EC56A33E04A2DA0423EBC63EBBD4E488C49BDC40</idno><idno type="DOI">10.1016/0022-2836(75)90187-4</idno><idno type="PII">0022-2836(75)90187-4</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1975</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The structure of purified phage λ repressor has been examined by high resolution electron microscopy. The repressor molecule appears predominantly as a tetramer of about 95 Å × 120 Å. We have proposed a model to account for the variety of aspects seen on the electron micrographs. Spreading DNA without protein film and use of uranyl formate staining allowed the simultaneous visualization of the DNA and the structure of the repressor molecule bound to it. Mapping the positions of λ repressor bound to whole λ DNA shows preferential binding to the region containing the operators. At high resolution multiple binding of repressor to the operator can be demonstrated. Depending on the amount of repressor present, rows of one to four repressor tetramers are seen on the DNA, confirming the model of the operator containing four binding sites for repressor. The bound repressor can consequently protect against nuclease digestion of operator pieces of approximately 30, 57, 87 and 111 base-pairs. 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The repressor molecule appears predominantly as a tetramer of about 95 Å × 120 Å. We have proposed a model to account for the variety of aspects seen on the electron micrographs. Spreading DNA without protein film and use of uranyl formate staining allowed the simultaneous visualization of the DNA and the structure of the repressor molecule bound to it. Mapping the positions of λ repressor bound to whole λ DNA shows preferential binding to the region containing the operators. At high resolution multiple binding of repressor to the operator can be demonstrated. Depending on the amount of repressor present, rows of one to four repressor tetramers are seen on the DNA, confirming the model of the operator containing four binding sites for repressor. The bound repressor can consequently protect against nuclease digestion of operator pieces of approximately 30, 57, 87 and 111 base-pairs. 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The repressor molecule appears predominantly as a tetramer of about 95 Å × 120 Å. We have proposed a model to account for the variety of aspects seen on the electron micrographs. Spreading DNA without protein film and use of uranyl formate staining allowed the simultaneous visualization of the DNA and the structure of the repressor molecule bound to it. Mapping the positions of λ repressor bound to whole λ DNA shows preferential binding to the region containing the operators. At high resolution multiple binding of repressor to the operator can be demonstrated. Depending on the amount of repressor present, rows of one to four repressor tetramers are seen on the DNA, confirming the model of the operator containing four binding sites for repressor. The bound repressor can consequently protect against nuclease digestion of operator pieces of approximately 30, 57, 87 and 111 base-pairs. 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