Skip to main content
Article
A Protein from Tetrahymena thermophila That Specifically Binds Parallel-Stranded G4-DNA
Biochemistry
  • Ted Schierer, Iowa State University
  • Eric Henderson, Iowa State University
Document Type
Article
Publication Version
Published Version
Publication Date
3-1-1994
DOI
10.1021/bi00174a034
Abstract
G4-DNA is a parallel, four-stranded structure mediated by tetrads of hydrogen-bonded guanines (G-quartets). An abundant protein called Tetrahymena G4 binding protein (TGP) that binds to an intermolecular, quadruplex form of d(TTGGGGTTGGGGTTGGGGTTGGGG) under physiological salt conditions has been identified in cellular extracts from the ciliated protozoan Tetrahymena thermophila. In binding competition experiments, molecules capable of forming G4 structures compete for binding to TGP, but non-G4-forming molecules and r(U2G4)4 do not. TGP binding also requires a single-stranded region adjacent to the G4 structure. During the course of this study, it was determined that Mg2+ facilitates the formation of parallel-stranded G4-DNA structures and that high oligonucleotide concentrations are not required to drive formation of these structures. In addition, G4-DNA and TGP/G4-DNA complexes form readily under physiological salt conditions. These data support the proposal that G4-DNA structures exist in vivo.
Comments

Reprinted (adapted) with permission from A Protein from Tetrahymena thermophila That Specifically Binds Parallel-Stranded G4-DNA. Ted Schierer and Eric Henderson. Biochemistry 1994 33 (8), 2240-2246. DOI: 10.1021/bi00174a034. Copyright 1994 American Chemical Society.

Copyright Owner
American Chemical Society
Language
en
File Format
application/pdf
Citation Information
Ted Schierer and Eric Henderson. "A Protein from Tetrahymena thermophila That Specifically Binds Parallel-Stranded G4-DNA" Biochemistry Vol. 33 Iss. 8 (1994) p. 2240 - 2246
Available at: http://works.bepress.com/eric-henderson/25/