Solution structure of telomere binding domain of AtTRB2 derived from Arabidopsis thaliana

Ji Hye Yun, Won Kyung Lee, Heeyoun Kim, Eunhee Kim, Chaejoon Cheong, Myeon Haeng Cho, Weon Tae Lee

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Telomere homeostasis is regulated by telomere-associated proteins, and the Myb domain is well conserved for telomere binding. AtTRB2 is a member of the SMH (Single-Myb-Histone)-like family in Arabidopsis thaliana, having an N-terminal Myb domain, which is responsible for DNA binding. The Myb domain of AtTRB2 contains three α-helices and loops for DNA binding, which is unusual given that other plant telomere-binding proteins have an additional fourth helix that is essential for DNA binding. To understand the structural role for telomeric DNA binding of AtTRB2, we determined the solution structure of the Myb domain of AtTRB2 (AtTRB2 1-64 ) using nuclear magnetic resonance (NMR) spectroscopy. In addition, the inter-molecular interaction between AtTRB2 1-64 and telomeric DNA has been characterized by the electrophoretic mobility shift assay (EMSA) and NMR titration analyses for both plant (TTTAGGG)n and human (TTAGGG)n telomere sequences. Data revealed that Trp28, Arg29, and Val47 residues located in Helix 2 and Helix 3 are crucial for DNA binding, which are well conserved among other plant telomere binding proteins. We concluded that although AtTRB2 is devoid of the additional fourth helix in the Myb-extension domain, it is able to bind to plant telomeric repeat sequences as well as human telomeric repeat sequences.

Original languageEnglish
Pages (from-to)436-442
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume452
Issue number3
DOIs
Publication statusPublished - 2014 Sep 26

Fingerprint

Telomere
Arabidopsis
DNA
Telomere-Binding Proteins
Plant Proteins
Magnetic Resonance Spectroscopy
Telomere Homeostasis
Electrophoretic mobility
Molecular interactions
Electrophoretic Mobility Shift Assay
Titration
Histones
Nuclear magnetic resonance spectroscopy
Assays
Nuclear magnetic resonance
Proteins

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Yun, Ji Hye ; Lee, Won Kyung ; Kim, Heeyoun ; Kim, Eunhee ; Cheong, Chaejoon ; Cho, Myeon Haeng ; Lee, Weon Tae. / Solution structure of telomere binding domain of AtTRB2 derived from Arabidopsis thaliana. In: Biochemical and Biophysical Research Communications. 2014 ; Vol. 452, No. 3. pp. 436-442.
@article{8a049563ecfa4d16b03f274f96954227,
title = "Solution structure of telomere binding domain of AtTRB2 derived from Arabidopsis thaliana",
abstract = "Telomere homeostasis is regulated by telomere-associated proteins, and the Myb domain is well conserved for telomere binding. AtTRB2 is a member of the SMH (Single-Myb-Histone)-like family in Arabidopsis thaliana, having an N-terminal Myb domain, which is responsible for DNA binding. The Myb domain of AtTRB2 contains three α-helices and loops for DNA binding, which is unusual given that other plant telomere-binding proteins have an additional fourth helix that is essential for DNA binding. To understand the structural role for telomeric DNA binding of AtTRB2, we determined the solution structure of the Myb domain of AtTRB2 (AtTRB2 1-64 ) using nuclear magnetic resonance (NMR) spectroscopy. In addition, the inter-molecular interaction between AtTRB2 1-64 and telomeric DNA has been characterized by the electrophoretic mobility shift assay (EMSA) and NMR titration analyses for both plant (TTTAGGG)n and human (TTAGGG)n telomere sequences. Data revealed that Trp28, Arg29, and Val47 residues located in Helix 2 and Helix 3 are crucial for DNA binding, which are well conserved among other plant telomere binding proteins. We concluded that although AtTRB2 is devoid of the additional fourth helix in the Myb-extension domain, it is able to bind to plant telomeric repeat sequences as well as human telomeric repeat sequences.",
author = "Yun, {Ji Hye} and Lee, {Won Kyung} and Heeyoun Kim and Eunhee Kim and Chaejoon Cheong and Cho, {Myeon Haeng} and Lee, {Weon Tae}",
year = "2014",
month = "9",
day = "26",
doi = "10.1016/j.bbrc.2014.08.095",
language = "English",
volume = "452",
pages = "436--442",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

Solution structure of telomere binding domain of AtTRB2 derived from Arabidopsis thaliana. / Yun, Ji Hye; Lee, Won Kyung; Kim, Heeyoun; Kim, Eunhee; Cheong, Chaejoon; Cho, Myeon Haeng; Lee, Weon Tae.

In: Biochemical and Biophysical Research Communications, Vol. 452, No. 3, 26.09.2014, p. 436-442.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Solution structure of telomere binding domain of AtTRB2 derived from Arabidopsis thaliana

AU - Yun, Ji Hye

AU - Lee, Won Kyung

AU - Kim, Heeyoun

AU - Kim, Eunhee

AU - Cheong, Chaejoon

AU - Cho, Myeon Haeng

AU - Lee, Weon Tae

PY - 2014/9/26

Y1 - 2014/9/26

N2 - Telomere homeostasis is regulated by telomere-associated proteins, and the Myb domain is well conserved for telomere binding. AtTRB2 is a member of the SMH (Single-Myb-Histone)-like family in Arabidopsis thaliana, having an N-terminal Myb domain, which is responsible for DNA binding. The Myb domain of AtTRB2 contains three α-helices and loops for DNA binding, which is unusual given that other plant telomere-binding proteins have an additional fourth helix that is essential for DNA binding. To understand the structural role for telomeric DNA binding of AtTRB2, we determined the solution structure of the Myb domain of AtTRB2 (AtTRB2 1-64 ) using nuclear magnetic resonance (NMR) spectroscopy. In addition, the inter-molecular interaction between AtTRB2 1-64 and telomeric DNA has been characterized by the electrophoretic mobility shift assay (EMSA) and NMR titration analyses for both plant (TTTAGGG)n and human (TTAGGG)n telomere sequences. Data revealed that Trp28, Arg29, and Val47 residues located in Helix 2 and Helix 3 are crucial for DNA binding, which are well conserved among other plant telomere binding proteins. We concluded that although AtTRB2 is devoid of the additional fourth helix in the Myb-extension domain, it is able to bind to plant telomeric repeat sequences as well as human telomeric repeat sequences.

AB - Telomere homeostasis is regulated by telomere-associated proteins, and the Myb domain is well conserved for telomere binding. AtTRB2 is a member of the SMH (Single-Myb-Histone)-like family in Arabidopsis thaliana, having an N-terminal Myb domain, which is responsible for DNA binding. The Myb domain of AtTRB2 contains three α-helices and loops for DNA binding, which is unusual given that other plant telomere-binding proteins have an additional fourth helix that is essential for DNA binding. To understand the structural role for telomeric DNA binding of AtTRB2, we determined the solution structure of the Myb domain of AtTRB2 (AtTRB2 1-64 ) using nuclear magnetic resonance (NMR) spectroscopy. In addition, the inter-molecular interaction between AtTRB2 1-64 and telomeric DNA has been characterized by the electrophoretic mobility shift assay (EMSA) and NMR titration analyses for both plant (TTTAGGG)n and human (TTAGGG)n telomere sequences. Data revealed that Trp28, Arg29, and Val47 residues located in Helix 2 and Helix 3 are crucial for DNA binding, which are well conserved among other plant telomere binding proteins. We concluded that although AtTRB2 is devoid of the additional fourth helix in the Myb-extension domain, it is able to bind to plant telomeric repeat sequences as well as human telomeric repeat sequences.

UR - http://www.scopus.com/inward/record.url?scp=84907535055&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84907535055&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2014.08.095

DO - 10.1016/j.bbrc.2014.08.095

M3 - Article

C2 - 25172657

AN - SCOPUS:84907535055

VL - 452

SP - 436

EP - 442

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -