How a single protein complex accommodates many different H/ACA RNAs.
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.
Meier
U Thomas
UT
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. meier@aecom.yu.edu
D000818:Animals; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019871:Dyskeratosis Congenita / Q000235:genetics / Q000378:metabolism*; D008322:Mammals / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary; D012326:RNA Splicing / Q000235:genetics; D012342:RNA, Small Nuclear / Q000235:genetics / Q000378:metabolism*; D020718:Ribonucleoproteins, Small Nucleolar / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D019843:Archaeal Proteins; C485802:GAR1 protein, human; D012342:RNA, Small Nuclear; D020718:Ribonucleoproteins, Small Nucleolar