Source:http://linkedlifedata.com/resource/pubmed/id/17919279
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2007-10-25
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pubmed:abstractText |
Bacterial RNase P is composed of an RNA subunit and a single protein (encoded by the rnpB and rnpA genes respectively). The Bacillus subtilis rnpA knockdown strain d7 was used to screen for functional conservation among bacterial RNase P proteins from a representative spectrum of bacterial subphyla. We demonstrate conserved function of bacterial RNase P (RnpA) proteins despite low sequence conservation. Even rnpA genes from psychrophilic and thermophilic bacteria rescued growth of B. subtilis d7 bacteria; likewise, terminal extensions and insertions between beta strands 2 and 3, in the so-called metal binding loop, were compatible with RnpA function in B. subtilis. A deletion analysis of B. subtilis RnpA defined the structural elements essential for bacterial RNase P function in vivo. We further extended our complementation analysis in B. subtilis strain d7 to the four individual RNase P protein subunits from three different Archaea, as well as to human Rpp21 and Rpp29 as representatives of eukaryal RNase P. None of these non-bacterial RNase P proteins showed any evidence of being able to replace the B. subtilis RNase P protein in vivo, supporting the notion that archaeal/eukaryal RNase P proteins are evolutionary unrelated to the bacterial RnpA protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
801-13
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pubmed:meshHeading |
pubmed-meshheading:17919279-Amino Acid Sequence,
pubmed-meshheading:17919279-Bacillus subtilis,
pubmed-meshheading:17919279-Bacterial Proteins,
pubmed-meshheading:17919279-Blotting, Western,
pubmed-meshheading:17919279-Evolution, Molecular,
pubmed-meshheading:17919279-Genetic Complementation Test,
pubmed-meshheading:17919279-Models, Molecular,
pubmed-meshheading:17919279-Molecular Sequence Data,
pubmed-meshheading:17919279-Mutation,
pubmed-meshheading:17919279-Phylogeny,
pubmed-meshheading:17919279-Protein Structure, Secondary,
pubmed-meshheading:17919279-Ribonuclease P,
pubmed-meshheading:17919279-Sequence Deletion
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pubmed:year |
2007
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pubmed:articleTitle |
Function of heterologous and truncated RNase P proteins in Bacillus subtilis.
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pubmed:affiliation |
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marbacher Weg 6, D-35037 Marburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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