| pubmed-article:10786845 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10786845 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:10786845 | lifeskim:mentions | umls-concept:C0008266 | lld:lifeskim |
| pubmed-article:10786845 | lifeskim:mentions | umls-concept:C0073243 | lld:lifeskim |
| pubmed-article:10786845 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:10786845 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10786845 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10786845 | pubmed:dateCreated | 2000-5-9 | lld:pubmed |
| pubmed-article:10786845 | pubmed:abstractText | The transfer RNA 5' maturation enzyme RNase P has been characterized in Bacteria, Archaea, and Eukarya. The purified enzyme from all three kingdoms is a ribonucleoprotein containing an essential RNA subunit; indeed, the RNA subunit of bacterial RNase P RNA is the sole catalytic component. In contrast, the RNase P activity isolated from spinach chloroplasts lacks an RNA component and appears to function as a catalytic protein. Nonetheless, the chloroplast enzyme recognizes a pre-tRNA substrate for E. coli RNase P and cleaves it as efficiently and precisely as does the bacterial enzyme. To ascertain whether there are differences in catalytic mechanism between an all-RNA and an all-protein RNase P, we took advantage of the fact that phosphodiester bond selection and hydrolysis by the E. coli RNase P ribozyme is directed by a Mg2+ ion coordinated to the nonbridging pro-Rp oxygen of the scissile bond, and is blocked by sulfur replacement of this oxygen. We therefore tested the ability of the chloroplast enzyme to process a precursor tRNA containing this sulfur substitution. Partially purified RNase P from spinach chloroplasts can accurately and efficiently process phosphorothioate-substituted pre-tRNAs; cleavage occurs exclusively at the thio-containing scissile bond. The enzymatic throughput is fivefold slower, consistent with a general chemical effect of the phosphorothioate substitution rather than with a metal coordination deficiency. The chloroplast RNase P reaction mechanism therefore does not involve a catalytic Mg2+ bonded to the pro-Rp phosphate oxygen, and hence is distinct from the mechanism of the bacterial ribozyme RNase P. | lld:pubmed |
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| pubmed-article:10786845 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10786845 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10786845 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10786845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10786845 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10786845 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10786845 | pubmed:issn | 1355-8382 | lld:pubmed |
| pubmed-article:10786845 | pubmed:author | pubmed-author:GegenheimerPP | lld:pubmed |
| pubmed-article:10786845 | pubmed:author | pubmed-author:LULL | lld:pubmed |
| pubmed-article:10786845 | pubmed:author | pubmed-author:ThomasB CBC | lld:pubmed |
| pubmed-article:10786845 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10786845 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:10786845 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10786845 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10786845 | pubmed:pagination | 545-53 | lld:pubmed |
| pubmed-article:10786845 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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| pubmed-article:10786845 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10786845 | pubmed:articleTitle | Chloroplast ribonuclease P does not utilize the ribozyme-type pre-tRNA cleavage mechanism. | lld:pubmed |
| pubmed-article:10786845 | pubmed:affiliation | Department of Molecular Biosciences, University of Kansas, Lawrence 66045-2106, USA. | lld:pubmed |
| pubmed-article:10786845 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10786845 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10786845 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
