Nucleic Acids Research, Vol 26, Issue 7 1613-1620, Copyright © 1998 by Oxford University Press
Q Lu, T Schierer, SG Kang and E Henderson
G-DNA, a polymorphic family of four-stranded DNA structures, has been
proposed to play roles in a variety of biological processes including
telomere function, meiotic recombination and gene regulation. Here we
report the purification and cloning of TGP1, a G-DNA specific binding
protein from Tetrahymena thermophila. TGP1 was purified by three-column
chromatographies, including a G-DNA affinity column. Two major proteins
(approximately 80 and approximately 40 kDa) were present in the most highly
purified column fraction. Renaturation experiments showed that the
approximately 80 kDa protein contains TGP1 activity. Biochemical
characterization showed that TGP1 is a G-DNA specific binding protein with
a preference for parallel G-DNAs. The TGP1/DNA complex has a dissociation
constant (Kd) of approximately 2.2 x 10(-8) M and TGP1 can form supershift
in gel mobility shift assays. The cDNA coding TGP1 was cloned and sequenced
based upon an internal peptide sequence obtained from the approximately 80
kDa protein. Sequence analyses showed that TGP1 is a basic protein with a
pI of 10.58, and contains two extensively hydrophilic and basic domains.
Homology searches revealed that TGP1 is a novel protein sharing weak
similarities with a number of proteins.
ARTICLES
Purification, characterization and molecular cloning of TGP1, a novel G- DNA binding protein from Tetrahymena thermophila
Department of Zoology and Genetics and Molecular, Cellular and Developmental Biology Program, Iowa State University, Ames, IA 50011, USA.
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