MAZ, a zinc finger protein, binds to c-MYC and C2 gene sequences regulating transcriptional initiation and termination.

• DOI: 10.1073/pnas.89.16.7452
• Publication Date: 2006-05-31T12:05:55Z
• Authors: S A Bossone; C Asselin; A J Patel; K B Marcu
• Keywords: Zinc finger nuclease; RING finger domain; Sp1 transcription factor; Transcription; LIM domain

ME1a1, a 16-base-pair nuclear factor binding site residing between the c-MYC P1 and P2 transcription initiation sites, is required for activity. A cDNA encoding 477-amino acid zinc finger protein designated MAZ (MYC-associated protein) was cloned from HeLa lambda gt11 library by screening with concatamerized ME1a1 probe. In addition to six potential fingers of Cys2His2 type, contains an amino-terminal proline-rich domain several polyalanine tracts. Its mRNA present in all human tissues tested except kidney, as doublet approximately 2.5 2.7 kilobases, along differentially expressed minor species. bound specifically wild-type sequence but not mutant that also failed yield When fusion pMAL-c vector, binds specificity GA box (GGGAGGG) found promoter, attenuator region within gene's first exon, related involved transcriptional termination C2 gene. may encode dual roles termination.