
Cocrystal structure of YY1 bound to the adeno-associated virus P5 initiator
Author(s) -
Hristo B. Houbaviy,
Anny Usheva,
Thomas Shenk,
S.K. Burley
Publication year - 1996
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.93.24.13577
Subject(s) - transcription (linguistics) , tata box , microbiology and biotechnology , polymerase , rna , yy1 , biology , transcription preinitiation complex , messenger rna , dna , promoter , chemistry , gene , genetics , gene expression , philosophy , linguistics
Ying–Yang 1 protein (YY1) supports specific, unidirectional initiation of messenger RNA production by RNA polymerase II from two adjacent start sites in the adeno-associated virus P5 promoter, a process which is independent of the TATA box-binding protein (TBP). The 2.5-Å resolution YY1-initiator element cocrystal structure reveals four zinc fingers recognizing a YY1-binding consensus sequence. Upstream of the transcription start sites protein–DNA contacts involve both strands and downstream they are virtually restricted to the template strand, permitting access to the active center of RNA polymerase II and ensuring specificity and directionality. The observed pattern of protein–DNA contacts also explains YY1 binding to a preformed transcription bubble, and YY1 binding to a DNA/RNA hybrid analog of the P5 promoter region containing a nascent RNA transcript. A model is proposed for YY1-directed, TBP-independent transcription initiation.