Abstract
Human nuclear RNase P purified from HeLa cells has ATPase activity. This activity is associated with one of the protein subunits of the enzyme, Rpp20. Thus, human nuclear RNase P, which contains several proteins and one essential RNA, has at least one other enzymatic activity in addition to cleavage of phosphoester bonds in RNA. The amino acid sequence of Rpp20 has a signature motif found in an ATPase-containing subunit of a family of protein complexes (ABC transporters) that mediate a variety of transmembrane traffic, as well as a segment, DlxxN, that resembles the DEAD box motif of many ATPases: together, these might represent an ATPase signature motif.
Original language | English (US) |
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Pages (from-to) | 441-444 |
Number of pages | 4 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 98 |
Issue number | 2 |
DOIs | |
State | Published - Jan 16 2001 |
Externally published | Yes |
Keywords
- ATPase inhibition
- ATPase motifs
- Rpp20
- tRNA precursor
ASJC Scopus subject areas
- General