| Literature DB >> 11583614 |
P Harnpicharnchai1, J Jakovljevic, E Horsey, T Miles, J Roman, M Rout, D Meagher, B Imai, Y Guo, C J Brame, J Shabanowitz, D F Hunt, J L Woolford.
Abstract
The pathway and complete collection of factors that orchestrate ribosome assembly are not clear. To address these problems, we affinity purified yeast preribosomal particles containing the nucleolar protein Nop7p and developed means to separate their components. Nop7p is associated primarily with 66S preribosomes containing either 27SB or 25.5S plus 7S pre-rRNAs. Copurifying proteins identified by mass spectrometry include ribosomal proteins, nonribosomal proteins previously implicated in 60S ribosome biogenesis, and proteins not known to be involved in ribosome production. Analysis of strains mutant for eight of these proteins not previously implicated in ribosome biogenesis showed that they do participate in this pathway. These results demonstrate that proteomic approaches in concert with genetic tools provide powerful means to purify and characterize ribosome assembly intermediates.Entities:
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Year: 2001 PMID： 11583614 DOI： 10.1016/s1097-2765(01)00344-6
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970