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B52  -  CG10851 gene product from transcript...

Drosophila melanogaster

Synonyms: 52 kDa bracketing protein, B52 protein, B52/SRp55, B52/dSRp55, CG10851, ...
 
 
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High impact information on B52

 

Biological context of B52

  • Thus, B52 is an essential gene and has a critical role in Drosophila development [5].
  • Microarray analyses revealed that many transcripts involved in brain organogenesis have altered splicing profiles upon both loss and gain of B52 function [6].
  • Almost all of the corresponding genes having a known function encode either transcription factors or components of signal transduction pathways, with the B52- binding fragments located to not only exonic but also intronic regions [7].
  • These results indicate that B52 has unique functions in the removal of some introns during development, and plays a critical role in cellular regulatory networks [7].
  • Drosophila SRp55 also functions as an alternative splicing factor in the human cell-free system [8].
 

Anatomical context of B52

  • Germ line transformation of Drosophila flies with B52 genomic DNA rescues this lethality [5].
 

Associations of B52 with chemical compounds

  • The omegaspeckles are distinct from interchromatin granules since nuclear speckles containing serine/arginine-rich SR-proteins like SC35 and SRp55 did not colocalize with the &ohgr; speckles [9].
  • In Chironomus tentans, hrp45 is an SR protein structurally similar to the Drosophila SRp55/B52 SR protein [10].
 

Other interactions of B52

  • The resulting deletion, B52(28), is confined to the B52 gene and its neighbor the Hrb87F gene [5].
  • Moreover, Kc cell nuclear extracts that were immunodepleted of B52 lost their ability to splice this ftz pre-mRNA [11].
  • Reexpression of the intronless copy of dE2F2 in B52-deficient cells restores the dE2F2-mediated repression [12].
 

Analytical, diagnostic and therapeutic context of B52

  • We have also examined the distribution of B52 on nonpolytene chromosomes in Drosophila cell cultures with an in vivo UV cross-linking method and find that, here too, B52 is associated with boundaries of transcriptionally active chromatin [1].

References

  1. Characterization of a Drosophila protein associated with boundaries of transcriptionally active chromatin. Champlin, D.T., Frasch, M., Saumweber, H., Lis, J.T. Genes Dev. (1991) [Pubmed]
  2. Analysis of the functional specificity of RS domains in vivo. Dauwalder, B., Mattox, W. EMBO J. (1998) [Pubmed]
  3. Identification and characterization of three members of the human SR family of pre-mRNA splicing factors. Screaton, G.R., Cáceres, J.F., Mayeda, A., Bell, M.V., Plebanski, M., Jackson, D.G., Bell, J.I., Krainer, A.R. EMBO J. (1995) [Pubmed]
  4. RNA aptamers as effective protein antagonists in a multicellular organism. Shi, H., Hoffman, B.E., Lis, J.T. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  5. The SR protein B52/SRp55 is essential for Drosophila development. Ring, H.Z., Lis, J.T. Mol. Cell. Biol. (1994) [Pubmed]
  6. The SR Family Proteins B52 and dASF/SF2 Modulate Development of the Drosophila Visual System by Regulating Specific RNA Targets. Gabut, M., Dejardin, J., Tazi, J., Soret, J. Mol. Cell. Biol. (2007) [Pubmed]
  7. Specific SR protein-dependent splicing substrates identified through genomic SELEX. Kim, S., Shi, H., Lee, D.K., Lis, J.T. Nucleic Acids Res. (2003) [Pubmed]
  8. Two members of a conserved family of nuclear phosphoproteins are involved in pre-mRNA splicing. Mayeda, A., Zahler, A.M., Krainer, A.R., Roth, M.B. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. Omega speckles - a novel class of nuclear speckles containing hnRNPs associated with noncoding hsr-omega RNA in Drosophila. Prasanth, K.V., Rajendra, T.K., Lal, A.K., Lakhotia, S.C. J. Cell. Sci. (2000) [Pubmed]
  10. A specific SR protein binds preferentially to the secretory protein gene transcripts in salivary glands of Chironomus tentans. Singh, O.P., Visa, N., Wieslander, L., Daneholt, B. Chromosoma (2006) [Pubmed]
  11. Pre-mRNA splicing by the essential Drosophila protein B52: tissue and target specificity. Hoffman, B.E., Lis, J.T. Mol. Cell. Biol. (2000) [Pubmed]
  12. Specific role of the SR protein splicing factor B52 in cell cycle control in Drosophila. Rasheva, V.I., Knight, D., Bozko, P., Marsh, K., Frolov, M.V. Mol. Cell. Biol. (2006) [Pubmed]
 
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