Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 22 (2-3), 81-5

Structural and Functional Similarities Between MRP and RNase P


Structural and Functional Similarities Between MRP and RNase P

R Reddy et al. Mol Biol Rep.


RNase P, the enzyme response for 5'-end processing of tRNAs and 4.5S RNA, has been extensively characterized from E. coli. The RNA component of E. coli RNase P, without the protein, has the enzymatic activity and is the first true RNA enzyme to be characterized. RNase P and MRP are two distinct nuclear ribonucleoprotein (RNP) particles characterized in many eukaryotic cells including human, yeast and plant cells. There are many similarities between RNase P and MRP. These include: (1) sequence specific endonuclease activity; (2) homology at the primary and secondary structure levels; and (3) common proteins in both the RNPs. It is likely that RNase P and MRP originated from a common ancestor.

Similar articles

See all similar articles

Cited by 12 PubMed Central articles

See all "Cited by" articles


    1. J Biol Chem. 1989 Sep 5;264(25):14835-9 - PubMed
    1. Mol Microbiol. 1991 Jul;5(7):1801-10 - PubMed
    1. Genes Dev. 1995 Feb 15;9(4):471-80 - PubMed
    1. Cell. 1983 Dec;35(3 Pt 2):849-57 - PubMed
    1. Proc Natl Acad Sci U S A. 1994 Jan 18;91(2):659-63 - PubMed

Publication types

MeSH terms