High impact information on SNF6

• Here, we present evidence that SNF6 has a more direct role in stimulating transcription than SNF2 and SNF5 [1].
• Previously, we showed that SNF2, SNF5, and SNF6 function interdependently in transcriptional activation, possibly forming a heteromeric complex [1].
• The N terminus of SNF6 contains a sequence homologous to nuclear localization signals and was sufficient to direct beta-galactosidase to the nucleus [2].
• The SNF6 coding sequence was identified by selective mutagenesis [2].
• Null mutations in SNF6 caused a wider range of pleiotropic defects than the previously isolated point mutation, including slow growth [2].

Biological context of SNF6

• These findings suggest roles for the SNF1 through SNF6 and SSN6 genes in the regulation of SUC2 gene expression by glucose repression [3].
• Construction of a frameshift mutation provided evidence that translational initiation at the second ATG yields a partially functional SNF6 product [2].
• Here we show that Snf6 and Snf5, two subunits of the SWI/SNF chromatin-remodeling complex in Saccharomyces cerevisiae, copurify with the NER damage-recognition heterodimer Rad4-Rad23 [4].

Other interactions of SNF6

• The ssn20 mutations also suppressed the defects in invertase derepression caused by snf5 and snf6 mutations, and selection for invertase-producing revertants of snf5 mutants yielded only additional ssn20 alleles [5].
• The SNF2, SNF5 and SNF6 genes are required for Ty transcription in Saccharomyces cerevisiae [6].
• Strains bearing a mutation in any of the SNF1-SNF6 genes cannot derepress secreted invertase synthesis, but did derepress PrB synthesis when grown in the absence of glucose [7].

Analytical, diagnostic and therapeutic context of SNF6

• A bifunctional SNF6-beta-galactosidase fusion protein was localized in the nucleus, as judged by immunofluorescence microscopy [2].

References