Title

A Tetrahymena thermophila G4-DNA Binding Protein with Dihydrolipoamide Dehydrogenase Activity

Campus Units

Zoology, Biochemistry, Biophysics and Molecular Biology

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

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