RNase P: Difference between revisions

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== Function ==

'''RNase P''' processing the 5′ end of pre-[[Transfer RNA (tRNA)|transfer RNAs]] as well as other RNA molecules.<ref>PMID:28697848</ref>. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref>

'''RNase P''' processing the 5′ end of pre-[[Transfer RNA (tRNA)|transfer RNAs]] as well as other RNA molecules.<ref>PMID:28697848</ref>. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein (RNP) complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref>

In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.<ref>PMID:19395864</ref> In yeast, the proteins of RNase P also bind telomerase.<ref>PMID:27156450</ref>

== Structural insights ==

The active site of RNase P contains metal ions. Specifically, in the ~~RNA~~-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of ''Arabidopsis'' proteinaceous RNase P.

The active site of RNase P contains metal ions. Specifically, in the RNP-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of ''Arabidopsis'' proteinaceous RNase P.

</StructureSection>

A topic page on the RNP-based ''S. cerevisiae'' RNase P is found [[yeast RNase P|here]]

== 3D Structures of RNase P ==

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 <StructureSection load='6ah3' size='350' side='right' caption=Yeast RNase P bound to pre-tRNA (PDB entry [[6ah3]])' scene='' pspeed='8>
 == Function ==
-'''RNase P''' processing the 5′ end of pre-[[Transfer RNA (tRNA)|transfer RNAs]] as well as other RNA molecules.<ref>PMID:28697848</ref>. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref>
+'''RNase P''' processing the 5′ end of pre-[[Transfer RNA (tRNA)|transfer RNAs]] as well as other RNA molecules.<ref>PMID:28697848</ref>. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein (RNP) complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref>
 In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.<ref>PMID:19395864</ref> In yeast, the proteins of RNase P also bind telomerase.<ref>PMID:27156450</ref>
 == Structural insights ==
-The active site of RNase P contains metal ions. Specifically, in the RNA-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of ''Arabidopsis'' proteinaceous RNase P.
+The active site of RNase P contains metal ions. Specifically, in the RNP-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of ''Arabidopsis'' proteinaceous RNase P.
 </StructureSection>
+A topic page on the RNP-based ''S. cerevisiae'' RNase P is found [[yeast RNase P|here]]
 == 3D Structures of RNase P ==