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Two types of spliceosomes catalyze splicing of pre-mRNAs.
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Recessive lethal point mutation leads to formation of aberrant U11- and U12-containing small nuclear ribonucleoproteins that impair the efficiency of U12-type splicing.
The authores propose that both the C-RRM folding defect and nonsense-mediated decay (NMD)-mediated decrease in the levels of the U11/U12-65K protein reduce formation of the U12-type intron recognition complex and missplicing of a subset of minor introns leading to pituitary hypoplasia and a subsequent defect in growth hormone secretion.
Study shows that the C-terminal RNA recognition motif of p65 binds to the distal 3' stem-loop of U6atac. By using a binary splice site mutation suppressor assay, results demonstrate that p65 protein-binding apical stem-loop of U12 snRNA can be replaced by this U6atac distal 3' stem-loop.
Exome analysis of one proband revealed missense (c.1320C>A, p.P474T) and nonsense (c.1504C>T, p.R502X) mutations in the RNPC3 gene.
U11/U12-65K contribute to di-snRNP (zeige LSM2 Proteine) formation and intron bridging in the minor prespliceosome
Two types of spliceosomes catalyze splicing of pre-mRNAs. The major U2-type spliceosome is found in all eukaryotes and removes U2-type introns, which represent more than 99% of pre-mRNA introns. The minor U12-type spliceosome is found in some eukaryotes and removes U12-type introns, which are rare and have distinct splice consensus signals. The U12-type spliceosome consists of several small nuclear RNAs and associated proteins. This gene encodes a 65K protein that is a component of the U12-type spliceosome. This protein contains two RNA recognition motifs (RRMs), suggesting that it may contact one of the small nuclear RNAs of the minor spliceosome.
RNA-binding region (RNP1, RRM) containing 3
, RNA-binding protein 40
, RNA recognition protein
, RNA-binding motif protein 40
, RNA-binding region-containing protein 3
, U11/U12 small nuclear ribonucleoprotein 65 kDa protein
, U11/U12 snRNP 65 kDa protein
, U11/U12 snRNP 65K