The Polypyrimidine Tract Binding (PTB) Protein Interacts With Single-Stranded DNA in a Sequence-Specific Manner
Author(s) -
Françoise Brunel,
Mario M. Zakin,
H. Buc,
Malcolm Buckle
Publication year - 1996
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/24.9.1608
Subject(s) - polypyrimidine tract binding protein , biology , dna , dna binding protein , microbiology and biotechnology , electrophoretic mobility shift assay , polypyrimidine tract , sequence (biology) , rna , rna binding protein , genetics , transcription factor , gene
Polypyrimidine tract binding (PTB) protein is a cellular factor whose function is unknown. Various RNA or single-stranded DNA sequences have been shown to interact with PTB. In this paper, using laser UV crosslinking and electrophoretic mobility shift assays to probe DNA-protein interactions, we demonstrate that PTB binding at a single-stranded DNA target is highly sequence-specific. We provide data showing that PTB interacts with the top strand of the adenovirus major late promoter transcriptional initiator, a sequence rich in pyrimidine residues. We also demonstrate that PTB is organised into at least two different binding domains.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom