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The lamin B receptor‐associated protein p34 shares sequence homology and antigenic determinants with the splicing factor 2‐associated protein p32
Author(s) -
George Simos,
Spyros D. Georgatos
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00479-x
Subject(s) - lamin , biology , rna splicing , nuclear lamina , peptide sequence , microbiology and biotechnology , nuclear protein , biochemistry , gene , transcription factor , rna
The lamin B receptor (p58) is an inner nuclear membrane protein that forms an in vivo complex with the nuclear lamins, a nuclear envelope kinase, and two other nuclear proteins with apparent M r of 18,000 (p18) and 34,000 (p34). We now report the isolation of p34 by partial dissociation of the immunoaffinity‐purified p58 protein complex. Determination of the N‐terminal amino acid sequence of purified p34 shows that this polypeptide is homologous to p32, a splicing factor 2 (SF2)‐associated protein. The relatedness between p34 and p32 can be further established by showing that antibodies raised against N‐ and C‐terminal peptides of p32 cross‐react with purified p34. As the amino acid sequence of p58 contains an arginine/serine (RS)‐rich region similar to the RS‐rich region found in SF 2, we speculate that these domains provide binding sites for p34 and that this protein may be a linker between the nuclear membrane and intranuclear spliceosomal substructures.