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Localization of residues in a novel DNA‐binding domain of DmSNAP43 required for DmSNAPc DNA‐binding activity
Author(s) -
Hung Ko-Hsuan,
Stumph William E.
Publication year - 2012
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/j.febslet.2012.02.009
Subject(s) - dna , b3 domain , dna binding domain , alanine scanning , binding domain , biology , mutagenesis , drosophila melanogaster , biochemistry , binding site , alanine , gene , chemistry , genetics , mutant , transcription factor , amino acid
Transcription of snRNA genes depends upon the recognition of the proximal sequence element (PSE) by the snRNA activating protein complex SNAPc. In Drosophila melanogaster , all subunits of DmSNAPc (DmSNAP43, DmSNAP50, and DmSNAP190) are required for PSE‐binding activity. Previous work demonstrated that a non‐canonical DmSNAP43 domain bounded by residues 193–272 was essential for DmSNAPc to bind to the PSE. In this study, the contribution of amino acid residues within this domain to DNA binding by DmSNAPc was investigated by alanine‐scanning mutagenesis. The results have identified two clusters of residues within this domain required for the sequence‐specific DNA‐binding activity of DmSNAPc.