| pubmed-article:12486455 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12486455 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:12486455 | lifeskim:mentions | umls-concept:C0995926 | lld:lifeskim |
| pubmed-article:12486455 | lifeskim:mentions | umls-concept:C0208356 | lld:lifeskim |
| pubmed-article:12486455 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12486455 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:12486455 | pubmed:dateCreated | 2002-12-17 | lld:pubmed |
| pubmed-article:12486455 | pubmed:abstractText | A gene encoding a putative ATP-dependent DNA ligase was identified in the genome of the hyperthermophilic archaeon Sulfolobus shibatae and expressed in Escherichia coli. The 601 amino acid recombinant polypeptide was a monomeric protein capable of strand joining on a singly nicked DNA substrate in the presence of ATP ( K(m)=34 micro mu) and a divalent cation (Mn(2+), Mg(2+), or Ca(2+)). dATP was partially active in supporting ligation catalyzed by the protein, but GTP, CTP, UTP, dGTP, dCTP, dTTP, and NAD(+) were inactive. The cloned Ssh ligase showed an unusual metal cofactor requirement; it was significantly more active in the presence of Mn(2+) than in the presence of Mg(2+) or Ca(2+). Unexpectedly, the native Ssh ligase preferred Mg(2+) and Ca(2+) rather than Mn(2+). Both native and recombinant enzymes displayed optimal nick-joining activity at 60-80 degrees C. Ssh ligase discriminated against substrates containing mismatches on the 3'-side of nick junction and was more tolerant of mismatches at the 5'-end than of those at the penultimate 5'-end. The enzyme showed little activity on a 1-nucleotide gapped substrate. This is the first biochemical study of a DNA ligase from the crenarchaeotal branch of the archaea domain. | lld:pubmed |
| pubmed-article:12486455 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12486455 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486455 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12486455 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12486455 | pubmed:issn | 1431-0651 | lld:pubmed |
| pubmed-article:12486455 | pubmed:author | pubmed-author:HuangLiL | lld:pubmed |
| pubmed-article:12486455 | pubmed:author | pubmed-author:LaiXiaoqinX | lld:pubmed |
| pubmed-article:12486455 | pubmed:author | pubmed-author:HaoFuyingF | lld:pubmed |
| pubmed-article:12486455 | pubmed:author | pubmed-author:ShaoHongbingH | lld:pubmed |
| pubmed-article:12486455 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12486455 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:12486455 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12486455 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12486455 | pubmed:pagination | 469-77 | lld:pubmed |
| pubmed-article:12486455 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12486455 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12486455 | pubmed:articleTitle | Biochemical characterization of an ATP-dependent DNA ligase from the hyperthermophilic crenarchaeon Sulfolobus shibatae. | lld:pubmed |
| pubmed-article:12486455 | pubmed:affiliation | State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People's Republic of China. | lld:pubmed |
| pubmed-article:12486455 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12486455 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12486455 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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