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		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2695398&amp;diff=337724</id>
		<title>PMID:2695398</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2695398&amp;diff=337724"/>
		<updated>2008-02-04T18:47:18Z</updated>

		<summary type="html">&lt;p&gt;74.192.196.125: New PMID: Page!&lt;/p&gt;
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&amp;lt;span style = &#039;font-size: large&#039;&amp;gt; &#039;&#039;&#039;Goodlove, PE, Cunningham, PR, Parker, J and Clark, DP&#039;&#039;&#039;  (1989) Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli.&#039;&#039;Gene&#039;&#039; &#039;&#039;&#039;85&#039;&#039;&#039;:209-14&amp;lt;/span&amp;gt;&lt;br /&gt;
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|{{TableHeadingColor}} |&#039;&#039;&#039;Abstract&#039;&#039;&#039; || A 6-kb fragment of DNA, which complemented defects in the alcohol dehydrogenase (ADH)-encoding gene (adhE) of Escherichia coli, was cloned into a multicopy vector. Both ADH and coenzyme-A-linked acetaldehyde dehydrogenase (ACDH) activities were encoded by the plasmid, pHIL8. The adhE gene was identified as an open reading frame of 891 codons encoding an Mr 96,008 protein (minus the initiating methionine). Codon usage analysis indicates that adhE should be highly expressed. This gene shows no significant homology to any previously sequenced ADH-encoding gene.&lt;br /&gt;
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|{{TableHeadingColor}} nowrap |&#039;&#039;&#039;Links&#039;&#039;&#039; ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=2695398 PubMed]&lt;br /&gt;
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		<author><name>74.192.196.125</name></author>
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:15178751&amp;diff=337723</id>
		<title>PMID:15178751</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:15178751&amp;diff=337723"/>
		<updated>2008-02-04T18:46:55Z</updated>

		<summary type="html">&lt;p&gt;74.192.196.125: New PMID: Page!&lt;/p&gt;
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&amp;lt;span style = &#039;font-size: large&#039;&amp;gt; &#039;&#039;&#039;Case, RB, Chang, YP, Smith, SB, Gore, J, Cozzarelli, NR and Bustamante, C&#039;&#039;&#039;  (2004) The bacterial condensin MukBEF compacts DNA into a repetitive, stable structure.&#039;&#039;Science&#039;&#039; &#039;&#039;&#039;305&#039;&#039;&#039;:222-7&amp;lt;/span&amp;gt;&lt;br /&gt;
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|{{TableHeadingColor}} |&#039;&#039;&#039;Abstract&#039;&#039;&#039; || Condensins are conserved proteins containing SMC (structural maintenance of chromosomes) moieties that organize and compact chromosomes in an unknown mechanism essential for faithful chromosome partitioning. We show that MukBEF, the condensin in Escherichia coli, cooperatively compacts a single DNA molecule into a filament with an ordered, repetitive structure in an adenosine triphosphate (ATP) binding-dependent manner. When stretched to a tension of approximately 17 piconewtons, the filament extended in a series of repetitive transitions in a broad distribution centered on 45 nanometers. A filament so extended and held at a lower force recondensed in steps of 35 nanometers or its multiples; this cycle was repeatable even in the absence of ATP and free MukBEF. Remarkably, the pattern of transitions displayed by a given filament during the initial extension was identical in every subsequent extension. Hence, after being deformed micrometers in length, each filament returned to its original compact structure without the addition of energy. Incubation with topoisomerase I increased the rate of recondensation and allowed the structure to extend and reform almost reversibly, indicating that supercoiled DNA is trapped in the condensed structure. We suggest a new model for how MukBEF organizes the bacterial chromosome in vivo.&lt;br /&gt;
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|{{TableHeadingColor}} nowrap |&#039;&#039;&#039;Links&#039;&#039;&#039; ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=15178751 PubMed]&lt;br /&gt;
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		<author><name>74.192.196.125</name></author>
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