Campus Units

Zoology

Document Type

Article

Publication Version

Published Version

Publication Date

1998

Journal or Book Title

Biochemistry

Volume

37

Issue

12

First Page

4224

Last Page

4234

DOI

10.1021/bi9716377

Abstract

G4-DNA is a four-stranded structure that is formed by guanine-rich sequences. We report here the purification and characterization of a novel G4-DNA binding protein from Tetrahymena thermophila, designated TGP2. TGP2 was found to preferentially bind to G4-DNA oligonucleotides with adjacent single-stranded domains containing phosphorylated 5‘ ends and the sequence element, 5‘-ACTG-3‘. The amino acid sequence of TGP2 has high similarity to dihydrolipoamide dehydrogenase (DLDH) from a variety of species, and TGP2 was shown to have DLDH activity. Purified DLDH from porcine heart and bovine intestinal mucosa were shown to bind specifically to G4-DNA oligonucleotides. On the basis of these results we conclude that TGP2 is DLDH in T. thermophila and suggest that the G4-DNA binding capability of TGP2/DLDH may be biologically relevant.

Comments

Reprinted (adapted) with permission from A Tetrahymena thermophila G4-DNA Binding Protein with Dihydrolipoamide Dehydrogenase Activity. Kehkooi Kee, Luming Niu, and Eric Henderson. Biochemistry 1998 37 (12), 4224-4234. DOI: 10.1021/bi9716377. Copyright 1998 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

Share

COinS