PUBLICATION
Solution structure of the Myb domain of Terfa derived from Zebrafish interacting with both human and plant telomeric DNA
- Authors
- Kim, M.J., Ko, Y.J., Yun, J.H., Lee, W.
- ID
- ZDB-PUB-210514-11
- Date
- 2021
- Source
- Biochemical and Biophysical Research Communications 559: 252-258 (Journal)
- Registered Authors
- Keywords
- Myb domain, Nuclear magnetic resonance, Telomere binding protein, Telomeric repeat binding factor a
- MeSH Terms
-
- Animals
- Base Sequence
- Binding Sites
- DNA, Plant/metabolism*
- Protein Binding
- Protein Domains
- Solutions
- Telomere/metabolism*
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/metabolism*
- PubMed
- 33984809 Full text @ Biochem. Biophys. Res. Commun.
Citation
Kim, M.J., Ko, Y.J., Yun, J.H., Lee, W. (2021) Solution structure of the Myb domain of Terfa derived from Zebrafish interacting with both human and plant telomeric DNA. Biochemical and Biophysical Research Communications. 559:252-258.
Abstract
Telomeric repeat binding factor a (Terfa) derived from zebrafish is a homologous protein with human telomeric repeat binding factor 2 (TRF2). Terfa is known as a senescence-associated biomarker in various research through the zebrafish animal model. In addition, according to the findings so far, it has been confirmed that human or plant telomere binding proteins bind to telomeric DNA specialized for each species, but, in our result, Terfa shows it strongly binds to both human or plant type telomeric DNA. Here we characterized the DNA binding properties and demonstrate the solution structure of Terfa and identified residues participating in the interaction with both human and plant telomeric DNA. In DNA recognition of human and plant telomere binding proteins, the N-terminal loop and the α-helix 3 part of Myb domain were bound majorly, whereas, in the case of Terfa, the N-terminal loop, the α-helix 1-2 loop, and α-helix 2 of the Myb domain were dominantly bound. Therefore, when Terfa recognizes DNA, it was found that the binding module differs from previously known telomere binding proteins. The comparison of the structure of the telomere binding proteins provides an opportunity to understand more specifically how the structural properties of each telomere binding protein are associated with telomeric DNA binding from an evolutionary point of view.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping