cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction - PubMed (original) (raw)

Comparative Study

cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction

T Lehmeier et al. Proc Natl Acad Sci U S A. 1994.

Abstract

The major small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/U6, and U5 share a set of common proteins denoted B/B', D1, D2, D3, E, F, and G which play an important part in the biogenesis of the snRNPs. In addition, there is a link between the common proteins and autoimmunity; the three D proteins, together with B/B', are the major autoantigens for the so-called anti-Sm antibodies often produced by patients suffering from systemic lupus erythematosus. Here we describe the characterization of the human proteins D2 and D3 by cDNA cloning and immunological methods. D2 and D3 are encoded by distinct genes and are 118 and 126 amino acids in length, respectively. Both proteins prepared by in vitro translation exhibit Sm epitopes and can be precipitated by anti-Sm autoantibodies. They react differently with various patient sera, in a manner consistent with the reaction pattern on immunoblots of the D proteins isolated from HeLa cells. D1 and D2 synthesized in vitro form specific complexes, a result that is significant for the assembly pathway of the various core proteins into an snRNP's core ribonucleoprotein structure. The D3 protein is homologous to the human D1 protein, showing an overall amino acid sequence identity of 29%, including two regions with over 60% identity. D2 has less than 15% sequence identity with D1 and D3. A data bank search revealed a striking similarity (with more than 40% sequence identity) between human D3 and a Saccharomyces cerevisiae gene, previously published as the 5' flanking gene of yeast pep3 [Preston, R.A., Manolson, M., Becherer, K., Weidenhammer, E., Kirkpatrick, D., Wright, R. & Jones, E. (1991) Mol. Cell. Biol. 11, 5801-5812], suggesting that this gene encodes the yeast homologue of the human D3 protein.

PubMed Disclaimer

Cited by

Spliceosomal U snRNP core assembly: Sm proteins assemble onto an Sm site RNA nonanucleotide in a specific and thermodynamically stable manner.
Raker VA, Hartmuth K, Kastner B, Lührmann R. Raker VA, et al. Mol Cell Biol. 1999 Oct;19(10):6554-65. doi: 10.1128/MCB.19.10.6554. Mol Cell Biol. 1999. PMID: 10490595 Free PMC article.
Interactions within the yeast Sm core complex: from proteins to amino acids.
Camasses A, Bragado-Nilsson E, Martin R, Séraphin B, Bordonné R. Camasses A, et al. Mol Cell Biol. 1998 Apr;18(4):1956-66. doi: 10.1128/MCB.18.4.1956. Mol Cell Biol. 1998. PMID: 9528767 Free PMC article.
Analysis of the autoantibody repertoire in Burkitt's lymphoma patients: frequent response against the transcription factor ATF-2.
Kersten C, Delabie J, Gaudernack G, Smeland EB, Fosså A. Kersten C, et al. Cancer Immunol Immunother. 2004 Dec;53(12):1119-26. doi: 10.1007/s00262-004-0558-0. Cancer Immunol Immunother. 2004. PMID: 15185015 Free PMC article.
snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions.
Hermann H, Fabrizio P, Raker VA, Foulaki K, Hornig H, Brahms H, Lührmann R. Hermann H, et al. EMBO J. 1995 May 1;14(9):2076-88. doi: 10.1002/j.1460-2075.1995.tb07199.x. EMBO J. 1995. PMID: 7744013 Free PMC article.

References

1. Proc Natl Acad Sci U S A. 1981 May;78(5):2737-41 - PubMed
1. FEBS Lett. 1989 Jul 3;250(2):585-90 - PubMed
1. Cell. 1984 Dec;39(3 Pt 2):499-509 - PubMed
1. Cell. 1985 Jan;40(1):111-8 - PubMed
1. Cell. 1985 Oct;42(3):751-8 - PubMed

cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction - PubMed (original) (raw)