Cloned Human snRNP Proteins B and B′ Differ Only in Their Carboxy-Terminal Part

Dam, Alje P. van; Winkel, I.N.; Zijstra-Baalbergen, J.; Smeenk, R. J. T.; Cuypers, H. T. M.

doi:10.1007/978-3-642-46681-6_7

Cited by 2 publications

(2 citation statements)

References 28 publications

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“…Human cells express two isoforms from the SNRPB gene, SmB (231 amino acids) and SmB′ (a.k.a. SmB1, 240 amino acids) by alternative splicing of the seventh (last) exon 13,14 . SmB and SmB′ differ at the C′‐terminal end in their last 2 and 11 amino acids, respectively.…”

Section: Introductionmentioning

confidence: 99%

Non‐ubiquitous expression of core spliceosomal protein SmB/B′ in chick and mouse embryos

Turner

Mellor

McElroy

et al. 2022

Developmental Dynamics

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Background Although splicing is an integral part of the expression of many genes in our body, genetic syndromes with spliceosomal defects affect only specific tissues. To help understand the mechanism, we investigated the expression pattern of a core protein of the major spliceosome, SmB/B′ (Small Nuclear Ribonucleoprotein Polypeptides B/B′), which is encoded by SNRPB. Loss‐of‐function mutations of SNRPB in humans cause cerebro‐costo‐mandibular syndrome (CCMS) characterized by rib gaps, micrognathia, cleft palate, and scoliosis. Our expression analysis focused on the affected structures as well as non‐affected tissues, using chick and mouse embryos as model animals. Results Embryos at young stages (gastrula) showed ubiquitous expression of SmB/B′. However, the level and pattern of expression became tissue‐specific as differentiation proceeded. The regions relating to CCMS phenotypes such as cartilages of ribs and vertebrae and palatal mesenchyme express SmB/B′ in the nucleus sporadically. However, cartilages that are not affected in CCMS also showed similar expressions. Another spliceosomal gene, SNRNP200, which mutations cause retinitis pigmentosa, was also prominently expressed in cartilages in addition to the retina. Conclusion The expression of SmB/B′ is spatiotemporally regulated during embryogenesis despite the ubiquitous requirement of the spliceosome, however, the expression pattern is not strictly correlated with the phenotype presentation.

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Section: Introductionmentioning

confidence: 99%

Non‐ubiquitous expression of core spliceosomal protein SmB/B′ in chick and mouse embryos

Turner

Mellor

McElroy

et al. 2022

Developmental Dynamics

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“…SmN/B/B’, SmD1, and SmD3 have C-terminal extensions that include symmetrically dimethylated RG repeats (Brahms et al, 2001; Tripsianes et al, 2011). The SmN/B/B’ C-terminal tails contain additional proline-rich sequences, where these regions in SmN, SmB and SmB’ are 93% homologous (van Dam et al, 1989). …”

Section: Introductionmentioning

confidence: 99%

Structural basis for the recognition of spliceosomal SmN/B/B’ proteins by the RBM5 OCRE domain in splicing regulation

Mourão

Bonnal

Soni

et al. 2016

eLife

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The multi-domain splicing factor RBM5 regulates the balance between antagonistic isoforms of the apoptosis-control genes FAS/CD95, Caspase-2 and AID. An OCRE (OCtamer REpeat of aromatic residues) domain found in RBM5 is important for alternative splicing regulation and mediates interactions with components of the U4/U6.U5 tri-snRNP. We show that the RBM5 OCRE domain adopts a unique β–sheet fold. NMR and biochemical experiments demonstrate that the OCRE domain directly binds to the proline-rich C-terminal tail of the essential snRNP core proteins SmN/B/B’. The NMR structure of an OCRE-SmN peptide complex reveals a specific recognition of poly-proline helical motifs in SmN/B/B’. Mutation of conserved aromatic residues impairs binding to the Sm proteins in vitro and compromises RBM5-mediated alternative splicing regulation of FAS/CD95. Thus, RBM5 OCRE represents a poly-proline recognition domain that mediates critical interactions with the C-terminal tail of the spliceosomal SmN/B/B’ proteins in FAS/CD95 alternative splicing regulation.

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Cloned Human snRNP Proteins B and B′ Differ Only in Their Carboxy-Terminal Part

Cited by 2 publications

References 28 publications

Non‐ubiquitous expression of core spliceosomal protein SmB/B′ in chick and mouse embryos

Non‐ubiquitous expression of core spliceosomal protein SmB/B′ in chick and mouse embryos

Structural basis for the recognition of spliceosomal SmN/B/B’ proteins by the RBM5 OCRE domain in splicing regulation

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