How a single protein complex accommodates many different H/ACA RNAs

Research output: Contribution to journalArticle

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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 languageEnglish (US)
Pages (from-to)311-315
Number of pages5
JournalTrends in Biochemical Sciences
Volume31
Issue number6
DOIs
StatePublished - Jun 2006

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Ribonucleoproteins
RNA
Dyskeratosis Congenita
Proteins
RNA Precursors
Telomere
Ribosomes
Bone
Crystal structure
Maintenance
Mutation
Bone Marrow failure syndromes

ASJC Scopus subject areas

  • Biochemistry

Cite this

How a single protein complex accommodates many different H/ACA RNAs. / Meier, U. Thomas.

In: Trends in Biochemical Sciences, Vol. 31, No. 6, 06.2006, p. 311-315.

Research output: Contribution to journalArticle

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