TY - JOUR
AU - 
AB - Downloaded from genesdev.cshlp.org on November 18, 2021 - Published by Cold Spring Harbor Laboratory Press Identification and purification of a 62,000-dalton protein that binds specifically to the polypyrimidine tract of introns Mariano A. Garcia-Blanco^ Sharon F. Jamison, and Phillip A. Sharp Center for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 USA A protein of molecular size 62,000 daltons (p62) was detected in HeLa cell nuclear extracts by UV cross-linking to mRNA precursors. p62 binds specifically to the polypyrimidine tract of the 3' splice site region of introns. p62 purified to homogeneity binds the polypyrimidine tract of pre-mRNAs. This binding does not require the AG dinucleotide at the 3' splice site. Alterations in the polypyrimidine tract that reduce the binding of p62 yield a corresponding reduction in the efficiency of formation of a U2 snRNP/pre-mRNA complex and splicing. The p62 protein is retained in the spliceosome, where it remains bound to the pre-mRNA. This polypyrimidine tract binding protein (pPTB) is proposed to be a critical component in recognition of the 3' splice site during splicing. [Key Words: Polypyrimidine tract; intron; 3' splice site; RNA-binding protein; UV cross-linking] Received August 24, 1989; revised version accepted 
TI - Identification and purification of a 62,000-dalton protein that binds specifically to the polypyrimidine tract of introns.
JF - Genes & Development
DO - 10.1101/gad.3.12a.1874
DA - 1989-12-01
UR - https://www.deepdyve.com/lp/unpaywall/identification-and-purification-of-a-62-000-dalton-protein-that-binds-4bC3v2kCvL
DP - DeepDyve
ER -