A protein subunit of human RNase P, Rpp14, and its interacting partner, OIP2, have 3′→5′ exoribonuclease activity
AUTOR(ES)
Jiang, Taijiao
FONTE
National Academy of Sciences
RESUMO
The processing of precursor tRNAs at their 5′ and 3′ termini is a fundamental event in the biosynthesis of tRNA. RNase P is generally responsible for endonucleolytic removal of a leader sequence of precursor tRNA to generate the mature 5′ terminus. However, much less is known about the RNase P counterparts or other proteins that are active at the tRNA 3′ terminus. Here we show that one of the human RNase P subunits, Rpp14, together with one of its interacting protein partners, OIP2, is a 3′→5′ exoribonuclease with a phosphorolytic activity that processes the 3′ terminus of precursor tRNA. Immunoprecipitates of a crude human RNase P complex can process both ends of precursor tRNA by hydrolysis, but purified RNase P has no exonuclease activity. Rpp14 and OIP2 may be part of an exosome activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=122763Documentos Relacionados
- Rpp2, an essential protein subunit of nuclear RNase P, is required for processing of precursor tRNAs and 35S precursor rRNA in Saccharomyces cerevisiae
- Characterization of the human and mouse WRN 3′→5′ exonuclease
- Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′→5′ exonuclease containing S1 and KH RNA-binding domains
- Y box-binding protein-1 binds preferentially to single-stranded nucleic acids and exhibits 3′→5′ exonuclease activity
- Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P