Resonance assignment and secondary structure of the tandem harmonin homology domains of human RTEL1

Kumar, N and Ghosh, M and Manikandan, P and Basak, S and Deepa, A and Singh, M (2022) Resonance assignment and secondary structure of the tandem harmonin homology domains of human RTEL1. In: Biomolecular NMR Assignments, 16 (1). pp. 159-164.

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Abstract

Regulator of telomere elongation helicase 1 (RTEL1) is an Fe-S cluster containing DNA helicase that plays important roles in telomere DNA maintenance, DNA repair, and genomic stability. It is a modular protein comprising an N-terminal helicase domain, two tandem harmonin homology domains 1 & 2 (HHD1 and HHD2), and a C-terminal C4C4 type RING domain. The N-terminal helicase domain disassembles the telomere t/D-loop and unwinds the G-quadruplex via its helicase activity. The C-terminal RING domain interacts with telomere DNA binding protein TRF2 and helps RTEL1 recruitment to the telomere. The tandem HHD1 and HHD2 are characterized as a putative protein-protein interaction domain and have recently been shown to interact with a DNA repair protein SLX4. Several mutations associated with Hoyeraal-Hreidarsson syndrome and pulmonary fibrosis have been found in HHD1 and HHD2 of RTEL1. However, these domains have not been characterized for their structures. We have expressed and purified HHD1 and HHD2 of human RTEL1 for their characterization using solution NMR spectroscopy. Here, we report near complete backbone and sidechain 1H, 13C and 15N chemical shift assignments and secondary structure of the HHD1 and HHD2 domains of human RTEL1.

Item Type:	Journal Article
Publication:	Biomolecular NMR Assignments
Publisher:	Springer Science and Business Media B.V.
Additional Information:	The copyright for this article belongs to the Springer Science and Business Media B.V.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	24 Jun 2022 11:54
Last Modified:	24 Jun 2022 11:54
URI:	https://eprints.iisc.ac.in/id/eprint/73703

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