| pubmed-article:17053064 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17053064 | lifeskim:mentions | umls-concept:C0600435 | lld:lifeskim |
| pubmed-article:17053064 | lifeskim:mentions | umls-concept:C0073243 | lld:lifeskim |
| pubmed-article:17053064 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:17053064 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:17053064 | pubmed:issue | 44 | lld:pubmed |
| pubmed-article:17053064 | pubmed:dateCreated | 2006-11-1 | lld:pubmed |
| pubmed-article:17053064 | pubmed:abstractText | RNase P, which catalyzes the magnesium-dependent 5'-end maturation of tRNAs in all three domains of life, is composed of one essential RNA and a varying number of protein subunits depending on the source: at least one in bacteria, four in archaea, and nine in eukarya. To address why multiple protein subunits are needed for archaeal/eukaryal RNase P catalysis, in contrast to their bacterial relative, in vitro reconstitution of these holoenzymes is a prerequisite. Using recombinant subunits, we have reconstituted in vitro the RNase P holoenzyme from the thermophilic archaeon Pyrococcus furiosus (Pfu) and furthered our understanding regarding its functional organization and assembly pathway(s). Whereas Pfu RNase P RNA (RPR) alone is capable of multiple turnover, addition of all four RNase P protein (Rpp) subunits to Pfu RPR results in a 25-fold increase in its k(cat) and a 170-fold decrease in K(m). In fact, even in the presence of only one of two specific pairs of Rpps, the RPR displays activity at lower substrate and magnesium concentrations. Moreover, a pared-down, mini-Pfu RNase P was identified with an RPR deletion mutant. Results from our kinetic and footprinting studies on Pfu RNase P, together with insights from recent structures of bacterial RPRs, provide a framework for appreciating the role of multiple Rpps in archaeal RNase P. | lld:pubmed |
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| pubmed-article:17053064 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17053064 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17053064 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17053064 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17053064 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17053064 | pubmed:author | pubmed-author:GopalanVenkat... | lld:pubmed |
| pubmed-article:17053064 | pubmed:author | pubmed-author:TsaiHsin-YueH... | lld:pubmed |
| pubmed-article:17053064 | pubmed:author | pubmed-author:PulukkunatDil... | lld:pubmed |
| pubmed-article:17053064 | pubmed:author | pubmed-author:WoznickWalter... | lld:pubmed |
| pubmed-article:17053064 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17053064 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:17053064 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:17053064 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17053064 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17053064 | pubmed:pagination | 16147-52 | lld:pubmed |
| pubmed-article:17053064 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17053064 | pubmed:meshHeading | pubmed-meshheading:17053064... | lld:pubmed |
| pubmed-article:17053064 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17053064 | pubmed:articleTitle | Functional reconstitution and characterization of Pyrococcus furiosus RNase P. | lld:pubmed |
| pubmed-article:17053064 | pubmed:affiliation | Molecular, Cellular and Developmental Biology Graduate Program, Ohio State Biochemistry Program, Ohio State University, Columbus, OH 43210, USA. | lld:pubmed |
| pubmed-article:17053064 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17053064 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17053064 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17053064 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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