Affordable Access

deepdyve-link
Publisher Website

Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain

Authors
  • Spåhr, Henrik
  • Samuelsson, Tore
  • Hällberg, B. Martin
  • Gustafsson, Claes M.
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Publication Date
Jan 01, 2010
Volume
397
Issue
3
Pages
386–390
Identifiers
DOI: 10.1016/j.bbrc.2010.04.130
Source
Elsevier
Keywords
License
Unknown

Abstract

In mammalian cells, a family of mitochondrial transcription termination factors (MTERFs) regulates mitochondrial gene expression. MTERF family members share a ∼270 residues long MTERF-domain required for DNA binding and transcription regulation. However, the structure of this widely conserved domain is unknown. Here, we show that the MTERF-domain of human MTERF3 forms a half-doughnut-shaped right-handed superhelix. The superhelix is built from α-helical tandem repeats that display a novel triangular three-helix motif. This repeat motif, which we denote the MTERF-motif, is a conserved structural element present in proteins from metazoans, plants, and protozoans. Furthermore, a narrow, strongly positively charged nucleic acid-binding path is found in the middle of the concave side of the half-doughnut. This arrangement suggests a half clamp nucleic acid-binding mode for MTERF-domains.

Report this publication

Statistics

Seen <100 times