pubmed-article:9882335 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9882335 | lifeskim:mentions | umls-concept:C0042216 | lld:lifeskim |
pubmed-article:9882335 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:9882335 | lifeskim:mentions | umls-concept:C0058605 | lld:lifeskim |
pubmed-article:9882335 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:9882335 | lifeskim:mentions | umls-concept:C0179400 | lld:lifeskim |
pubmed-article:9882335 | lifeskim:mentions | umls-concept:C1256786 | lld:lifeskim |
pubmed-article:9882335 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9882335 | pubmed:dateCreated | 1999-2-18 | lld:pubmed |
pubmed-article:9882335 | pubmed:abstractText | Vaccinia virus nucleoside triphosphate phosphohydrolase I (NPH-I) is a DNA-dependent ATPase that serves as a transcription termination factor during viral mRNA synthesis. NPH-I is a member of the DExH box family of nucleic acid-dependent nucleoside triphosphatases (NTPases), which is defined by the presence of several conserved sequence motifs. We have assessed the contributions of individual amino acids (underlined) in motifs I (GxGKT), II (DExHN), III (SAT), and VI (QxxGRxxR) to ATP hydrolysis by performing alanine scanning mutagenesis. Significant decrements in ATPase activity resulted from mutations at nine positions: Lys-61 and Thr-62 (motif I); Asp-141, Glu-142, His-144, and Asn-145 (motif II); and Gln-472, Arg-476, and Arg-479 (motif VI). Structure-function relationships at each of these positions were clarified by introducing conservative substitutions and by steady-state kinetic analysis of the mutant enzymes. Comparison of our findings for NPH-I with those of mutational studies of other DExH and DEAD box proteins underscores similarities as well as numerous disparities in structure-activity relationships. We conclude that the functions of the conserved amino acids of the NTPase motifs are context dependent. | lld:pubmed |
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pubmed-article:9882335 | pubmed:language | eng | lld:pubmed |
pubmed-article:9882335 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9882335 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9882335 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9882335 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9882335 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:9882335 | pubmed:author | pubmed-author:ShumanSS | lld:pubmed |
pubmed-article:9882335 | pubmed:author | pubmed-author:MartinyGG | lld:pubmed |
pubmed-article:9882335 | pubmed:author | pubmed-author:GrossC HCH | lld:pubmed |
pubmed-article:9882335 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9882335 | pubmed:volume | 73 | lld:pubmed |
pubmed-article:9882335 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9882335 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9882335 | pubmed:pagination | 1302-8 | lld:pubmed |
pubmed-article:9882335 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:9882335 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:9882335 | pubmed:articleTitle | Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase I, a DNA-dependent ATPase of the DExH box family. | lld:pubmed |
pubmed-article:9882335 | pubmed:affiliation | Molecular Biology Program, Sloan-Kettering Institute, New York, New York 10021, USA. | lld:pubmed |
pubmed-article:9882335 | pubmed:publicationType | Journal Article | lld:pubmed |
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