| pubmed-article:10715140 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10715140 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:10715140 | lifeskim:mentions | umls-concept:C1510699 | lld:lifeskim |
| pubmed-article:10715140 | lifeskim:mentions | umls-concept:C0178555 | lld:lifeskim |
| pubmed-article:10715140 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:10715140 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:10715140 | pubmed:dateCreated | 2000-4-14 | lld:pubmed |
| pubmed-article:10715140 | pubmed:abstractText | Escherichia coli MutS protein, which is required for mismatch repair, has a slow ATPase activity that obeys Michalelis-Menten kinetics. At 37 degrees C, the steady-state turnover rate for ATP hydrolysis is 1.0 +/- 0.3 min(-1) per monomer equivalent with a K(m) of 33 +/- 6 microM. Hydrolysis is competitively inhibited by the ATP analogues AMPPNP and ATPgammaS, with K(i) values of 4 microM in both cases, and by ADP with a K(i) of 40 microM. The rate of ATP hydrolysis is stimulated 2-5-fold by short hetero- and homoduplex DNAs. The concentration of DNA cofactor that yields half-maximal stimulation is lowest for oligodeoxynucleotide duplexes that contain a mismatched base pair. Pre-steady-state chemical quench analysis has demonstrated a substoichiometric initial burst of ADP formation by free MutS that is governed by a rate constant of 78 min(-1), indicating that the rate-limiting step for the steady-state reaction occurs after hydrolysis. Prebinding of MutS to homoduplex DNA does not alter the burst kinetics or amplitude but only increases the steady-state rate. In contrast, binding of the protein to heteroduplex DNA abolishes the burst of ADP formation, indicating that the rate-limiting step now occurs before hydrolysis. Gel filtration analysis indicates that the MutS dimer assembles into higher order oligomers in a concentration-dependent manner, and that ATP binding shifts this equilibrium to favor assembly. These results, together with kinetic findings, indicate nonequivalence of subunits within a MutS oligomer with respect to ATP hydrolysis and DNA binding. | lld:pubmed |
| pubmed-article:10715140 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10715140 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10715140 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10715140 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10715140 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10715140 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10715140 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10715140 | pubmed:author | pubmed-author:ModrichPP | lld:pubmed |
| pubmed-article:10715140 | pubmed:author | pubmed-author:AllenD JDJ | lld:pubmed |
| pubmed-article:10715140 | pubmed:author | pubmed-author:BjornsonK PKP | lld:pubmed |
| pubmed-article:10715140 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10715140 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:10715140 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:10715140 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10715140 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10715140 | pubmed:pagination | 3176-83 | lld:pubmed |
| pubmed-article:10715140 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10715140 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10715140 | pubmed:articleTitle | Modulation of MutS ATP hydrolysis by DNA cofactors. | lld:pubmed |
| pubmed-article:10715140 | pubmed:affiliation | Department of Biochemistry and Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:10715140 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10715140 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10715140 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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