Protein-protein interactions with subunits of human nuclear RNase P

T. Altman, S. Altman

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

A yeast two-hybrid system was used to analyze interactions among the protein subunits of human nuclear RNase P themselves and with other interacting partners encoded in a HeLa cell cDNA library. Subunits hpop1, Rpp21, Rpp29, Rpp30, Rpp38, and Rpp40 are involved in extensive, but weak, protein-protein interactions in the holoenzyme complex. Rpp14, Rpp20, and Rpp30 were found to have strong interactions with proteins encoded in the cDNA library. The small heat shock protein 27, which interacts with Rpp20 in the two-hybrid assay, binds to Rpp20 during affinity chromatography and can be found to be associated with, and enhances the activity of, highly purified RNase P. RNase P activity in HeLa cell nuclei also increases under the stress of heat shock.

Original languageEnglish (US)
Pages (from-to)920-925
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number3
DOIs
StatePublished - Jan 30 2001
Externally publishedYes

Keywords

  • Heat shock
  • Hsp27
  • Nuclear proteins
  • Precursor tRNA

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Protein-protein interactions with subunits of human nuclear RNase P'. Together they form a unique fingerprint.

  • Cite this