Abstract
More than 100 mammalian H/ACA RNAs form an equal number of ribonucleoproteins (RNPs) by associating with the same four core proteins. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes. Recent crystal structures of archaeal H/ACA protein complexes show how the same four proteins accommodate >100 distinct but related H/ACA RNAs and reveal that a spatial mutation cluster underlies dyskeratosis congenita, a syndrome of bone marrow failure.
Original language | English (US) |
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Pages (from-to) | 311-315 |
Number of pages | 5 |
Journal | Trends in Biochemical Sciences |
Volume | 31 |
Issue number | 6 |
DOIs | |
State | Published - Jun 2006 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology