Comment
doi: 10.1073/pnas.0611193104.
Epub 2007 Feb 7.
Uniformity amid diversity in RNase P
Affiliations
- PMID: 17287341
- PMCID: PMC1892978
- DOI: 10.1073/pnas.0611193104
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Comment
Uniformity amid diversity in RNase P
Proc Natl Acad Sci U S A.
.
No abstract available
Conflict of interest statement
The author declares no conflict of interest.
Figures
Function and subunit composition of RNase P. (A) The reaction catalyzed by RNase P. (B–E) Universally conserved nucleotides are depicted in the secondary structures of representative RPRs from the three domains of life (17). Of the various structural elements, only the P4 helix is labeled. In B and C, the pared-down catalytic domains that are active in the presence of their cognate Rpps are shown in black. In bacterial RPR, blue indicates the substrate-specificity domain, and red lines indicate experimentally validated tertiary contacts. Archaeal RPRs are classified as types A (ancestral version; C) and M (those primarily from Methanococci; D); the latter have not been proven to be active in the absence of cognate Rpps (7).
Comment on
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Eukaryotic RNase P RNA mediates cleavage in the absence of protein.Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2062-7. doi: 10.1073/pnas.0607326104. Epub 2007 Feb 6. Proc Natl Acad Sci U S A. 2007. PMID: 17284611 Free PMC article.
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