pubmed-article:14530447 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C1823153 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C2349976 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C1552644 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C0587267 | lld:lifeskim |
pubmed-article:14530447 | lifeskim:mentions | umls-concept:C1481621 | lld:lifeskim |
pubmed-article:14530447 | pubmed:issue | 20 | lld:pubmed |
pubmed-article:14530447 | pubmed:dateCreated | 2003-10-7 | lld:pubmed |
pubmed-article:14530447 | pubmed:abstractText | R6K-encoded pi protein can bind to the seven, 22 bp tandem iterons of the gamma origin. In this work, we use a variant of pi, His-pi.F107S, that is hyperactive in replication. In vitro, His-pi.F107S-dependent local DNA melting (open complex formation) occurs in the absence of host proteins (IHF/HU or DnaA) and it is positioned in the A + T-rich region adjacent to iterons. Experiments described here examine the effects of ATP, Mg2+ and temperature on the opening reaction. We show that the opening of the gamma origin can occur in the presence of ATP as well as AMP-PCP (a non-hydrolyzable ATP analog). This suggests that, for gamma origin, ATP hydrolysis may be unnecessary for open complex formation facilitated by His-pi.F107S. In the absence of ATP or Mg2+, His-pi.F107S yielded data suggestive of distortions in the iteron attributable to DNA bending rather than DNA melting. Our findings also demonstrate that ATP and pi stimulate open complex formation over a wide range of temperatures, but not at 0 degrees C. These and other results indicate that ATP and/or Mg2+ are not needed for His-pi.F107S binding to iterons and that ATP effects an allosteric change in the protein bound to gamma origin. | lld:pubmed |
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pubmed-article:14530447 | pubmed:language | eng | lld:pubmed |
pubmed-article:14530447 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14530447 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14530447 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:14530447 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14530447 | pubmed:month | Oct | lld:pubmed |
pubmed-article:14530447 | pubmed:issn | 1362-4962 | lld:pubmed |
pubmed-article:14530447 | pubmed:author | pubmed-author:FilutowiczMar... | lld:pubmed |
pubmed-article:14530447 | pubmed:author | pubmed-author:KrügerRicardo... | lld:pubmed |
pubmed-article:14530447 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:14530447 | pubmed:day | 15 | lld:pubmed |
pubmed-article:14530447 | pubmed:volume | 31 | lld:pubmed |
pubmed-article:14530447 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14530447 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14530447 | pubmed:pagination | 5993-6003 | lld:pubmed |
pubmed-article:14530447 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:14530447 | pubmed:meshHeading | pubmed-meshheading:14530447... | lld:pubmed |
pubmed-article:14530447 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14530447 | pubmed:articleTitle | pi protein- and ATP-dependent transitions from 'closed' to 'open' complexes at the gamma ori of plasmid R6K. | lld:pubmed |
pubmed-article:14530447 | pubmed:affiliation | Department of Bacteriology, University of Wisconsin-Madison, 420 Henry Mall, Madison, WI 53706, USA. | lld:pubmed |
pubmed-article:14530447 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14530447 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:14530447 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |