A subunit of human nuclear RNase P has ATPase activity

Y. Li, S. Altman

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


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 languageEnglish (US)
Pages (from-to)441-444
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number2
StatePublished - Jan 16 2001
Externally publishedYes


  • ATPase inhibition
  • ATPase motifs
  • Rpp20
  • tRNA precursor

ASJC Scopus subject areas

  • General


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