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Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nagadoi, Aritaka Nishimura, Yoshifumi Hanaoka, Shingo
Description	Country affiliation: Japan Author Affiliation: Hanaoka S ( Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan.)
Abstract	Mammalian telomeres consist of long tandem arrays of double-stranded telomeric TTAGGG repeats packaged by the telomeric DNA-binding proteins TRF1 and TRF2. Both contain a similar C-terminal Myb domain that mediates sequence-specific binding to telomeric DNA. In a DNA complex of TRF1, only the single Myb-like domain consisting of three helices can bind specifically to double-stranded telomeric DNA. TRF2 also binds to double-stranded telomeric DNA. Although the DNA binding mode of TRF2 is likely identical to that of TRF1, TRF2 plays an important role in the t-loop formation that protects the ends of telomeres. Here, to clarify the details of the double-stranded telomeric DNA-binding modes of TRF1 and TRF2, we determined the solution structure of the DNA-binding domain of human TRF2 bound to telomeric DNA; it consists of three helices, and like TRF1, the third helix recognizes TAGGG sequence in the major groove of DNA with the N-terminal arm locating in the minor groove. However, small but significant differences are observed; in contrast to the minor groove recognition of TRF1, in which an arginine residue recognizes the TT sequence, a lysine residue of TRF2 interacts with the TT part. We examined the telomeric DNA-binding activities of both DNA-binding domains of TRF1 and TRF2 and found that TRF1 binds more strongly than TRF2. Based on the structural differences of both domains, we created several mutants of the DNA-binding domain of TRF2 with stronger binding activities compared to the wild-type TRF2.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	14
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2005-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chemistry Telomere Telomeric Repeat Binding Protein 1 Telomeric Repeat Binding Protein 2 Binding Sites Metabolism Models, Molecular Mutation Protein Conformation Protein Structure, Tertiary Comparative Study Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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