| pubmed-article:10429188 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10429188 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10429188 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10429188 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:10429188 | lifeskim:mentions | umls-concept:C0242506 | lld:lifeskim |
| pubmed-article:10429188 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10429188 | pubmed:dateCreated | 1999-8-17 | lld:pubmed |
| pubmed-article:10429188 | pubmed:abstractText | Structural studies of the proteins of the BstVI restriction-modification system of Bacillus stearothermophilus V were carried out using intrinsic fluorescence techniques. The exposure and environments of their tryptophanyl residues were determined using collisional quenchers. Quenching of BstVI endonuclease by iodide suggested a heterogeneous class of tryptophan residues, while the results obtained with M.BstVI methylase were consistent with a rather exposed tryptophan population. A comparison of the quenching efficiencies at 20 degrees C and 55 or 60 degrees C showed that their structures are more flexible and open at the temperature at which they exhibit maximal activity. The endonuclease reached its active conformation only after 1 h of incubation at 60 degrees C. Fluorescence changes were observed upon Mn2+ and Mg2+ binding, with Kd values in the range 3-5 microM. The binding of S-adenosyl-L-methionine to the methylase produced conformational changes, which were consistent with binding to a single site of Kd 550 and 680 microM at 20 degrees C and 55 degrees C, respectively. Quenching experiments with iodide showed that the presence of S-adenosyl-L-methionine leads to different conformational states at 20 degrees C and 55 degrees C. These results were interpreted in terms of differences in the structural characteristics of these restriction-modification proteins as well as in terms of differences in the conformational states that these enzymes exhibit at 20 degrees C and at the temperature at which they are most active. | lld:pubmed |
| pubmed-article:10429188 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10429188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10429188 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10429188 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10429188 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:10429188 | pubmed:author | pubmed-author:VásquezCC | lld:pubmed |
| pubmed-article:10429188 | pubmed:author | pubmed-author:SaavedraCC | lld:pubmed |
| pubmed-article:10429188 | pubmed:author | pubmed-author:EncinasM VMV | lld:pubmed |
| pubmed-article:10429188 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10429188 | pubmed:volume | 263 | lld:pubmed |
| pubmed-article:10429188 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10429188 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10429188 | pubmed:pagination | 65-70 | lld:pubmed |
| pubmed-article:10429188 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:meshHeading | pubmed-meshheading:10429188... | lld:pubmed |
| pubmed-article:10429188 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10429188 | pubmed:articleTitle | Structural studies of the BstVI restriction-modification proteins by fluorescence spectroscopy. | lld:pubmed |
| pubmed-article:10429188 | pubmed:affiliation | Facultad de Química y Biología, Universidad de Santiago de Chile, Santiago, Chile. | lld:pubmed |
| pubmed-article:10429188 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10429188 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10429188 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
