Literature DB >> 2146160

Analysis of U1snRNP-specific A protein cross-linked complexes.

J Boix1, W J Habets, W J van Venrooij, H C Smith.   

Abstract

The organization of the U1snRNP-specific A protein (34 kDa) has been analyzed by 12 and 16 A thiol-reversible chemical cross-linking and Western blotting. A-containing cross-linked complexes had molecular masses of 43, 47, 56, 62, 67, 105 and 125 kDa. None of these complexes could be cross-linked following ribonuclease digestion, suggesting that UsnRNA may play important roles in the spatial organization of A and other proteins. Moreover, the data suggest that A is proximal to, and may have interactions with, UsnRNP-specific proteins C and 70 kDa as well as with UsnRNP-common proteins B, E and G.

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Year:  1990        PMID: 2146160     DOI: 10.1016/0014-5793(90)80487-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Sex-lethal interacts with splicing factors in vitro and in vivo.

Authors:  G Deshpande; M E Samuels; P D Schedl
Journal:  Mol Cell Biol       Date:  1996-09       Impact factor: 4.272

2.  Structure of the small nuclear RNP particle U1: identification of the two structural protuberances with RNP-antigens A and 70K.

Authors:  B Kastner; U Kornstädt; M Bach; R Lührmann
Journal:  J Cell Biol       Date:  1992-02       Impact factor: 10.539

  2 in total

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