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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Snr1  -  Snf5-related 1

Drosophila melanogaster

Synonyms: BAP45, CG1064, Dmel\CG1064, SNR1, Snr, ...
 
 
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High impact information on Snr1

  • We show that Brm complex mutants suppress the DmcycE(JP) phenotype by increasing S phases without affecting DmcycE protein levels and that DmcycE physically interacts with Brm and Snr1 in vivo [1].
  • We performed yeast two hybrid screening of Drosophila cDNA library and detected interaction between a TRX polypeptide spanning SET and the SNR1 protein [2].
  • Epitope-tagged SNR1 was detected at discrete sites on larval salivary gland polytene chromosomes, and these sites colocalized with around one-half of TRX binding sites [2].
  • The Drosophila SNR1 (SNF5/INI1) subunit directs essential developmental functions of the Brahma chromatin remodeling complex [3].
  • We identified a temperature-sensitive allele of snr1 caused by a single amino acid substitution in the conserved repeat 2 region, implicated in a variety of protein-protein interactions [3].
 

Biological context of Snr1

  • BRM encodes the catalytic ATPase required for chromatin remodeling and SNR1 is a regulatory subunit [4].
  • Temperature shifts show that snr1 is continuously required, with essential functions in embryogenesis, pupal stages, and adults [3].
  • Expression of SNR1 transgenes revealed unexpected roles in wing patterning, abdomen development, oogenesis, and sustained adult viability [5].
  • A widespread distribution of SNR1 and BRM on the salivary gland polytene chromosomes showed that the Brm complex associated with many genes, but not always at transcribed loci, consistent with genetic data suggesting roles in both gene activation and repression [5].
  • Further, disrupting snr1 function suppressed DmcycEJP phenotypes, and increased cell growth defects associated with the conditional snr1E1 mutant were suppressed by reducing DmcycE levels [6].
 

Regulatory relationships of Snr1

  • Despite essential Brm complex functions in leg development, genetic and protein localization studies revealed that snr1 was not required or expressed in all tissues dependent on Brm complex activities [5].
 

Other interactions of Snr1

  • The SNR1-mediated repression is dependent on cooperation with histone deacetylases (HDAC) and physical associations with NET, a localized vein repressor [7].
 

Analytical, diagnostic and therapeutic context of Snr1

References

  1. Drosophila cyclin E interacts with components of the Brahma complex. Brumby, A.M., Zraly, C.B., Horsfield, J.A., Secombe, J., Saint, R., Dingwall, A.K., Richardson, H. EMBO J. (2002) [Pubmed]
  2. The C-terminal SET domains of ALL-1 and TRITHORAX interact with the INI1 and SNR1 proteins, components of the SWI/SNF complex. Rozenblatt-Rosen, O., Rozovskaia, T., Burakov, D., Sedkov, Y., Tillib, S., Blechman, J., Nakamura, T., Croce, C.M., Mazo, A., Canaani, E. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  3. The Drosophila SNR1 (SNF5/INI1) subunit directs essential developmental functions of the Brahma chromatin remodeling complex. Marenda, D.R., Zraly, C.B., Feng, Y., Egan, S., Dingwall, A.K. Mol. Cell. Biol. (2003) [Pubmed]
  4. Hormone-response Genes Are Direct in Vivo Regulatory Targets of Brahma (SWI/SNF) Complex Function. Zraly, C.B., Middleton, F.A., Dingwall, A.K. J. Biol. Chem. (2006) [Pubmed]
  5. SNR1 is an essential subunit in a subset of Drosophila brm complexes, targeting specific functions during development. Zraly, C.B., Marenda, D.R., Nanchal, R., Cavalli, G., Muchardt, C., Dingwall, A.K. Dev. Biol. (2003) [Pubmed]
  6. SNR1 (INI1/SNF5) mediates important cell growth functions of the Drosophila Brahma (SWI/SNF) chromatin remodeling complex. Zraly, C.B., Marenda, D.R., Dingwall, A.K. Genetics (2004) [Pubmed]
  7. The Drosophila Brahma (SWI/SNF) chromatin remodeling complex exhibits cell-type specific activation and repression functions. Marenda, D.R., Zraly, C.B., Dingwall, A.K. Dev. Biol. (2004) [Pubmed]
  8. dDYRK2 and Minibrain interact with the chromatin remodelling factors SNR1 and TRX. Kinstrie, R., Lochhead, P.A., Sibbet, G., Morrice, N., Cleghon, V. Biochem. J. (2006) [Pubmed]
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