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. 2018 Jan 4;46(5):2308–2320. doi: 10.1093/nar/gkx1302

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Overview over the domain organization of archaeal TFE subunits and related eukaryotic proteins. TFEα-related proteins are composed of extended winged-helix domains (eWH), a zinc ribbon domain (ZR) and coiled coil helices (CC) (3–5,55). TFEβ-related proteins are composed of winged-helix (WH) and iron-sulphur cluster domains (FeS). Sequence alignments of the two metal binding domains (ZR and FeS) reveal the loss of cysteine residues (highlighted in yellow) required for metal coordination in H. volcanii TFEα and TFEβ. Key to sequences: H. sapiens TFIIEα (NCBI accession: P29083), S. cerevisiae Tfa1 (EDN59878), S. solfataricus TFEα (AAK40605), M. jannaschii TFE (Q58187), H. salinarum TFEα (AAG19231), H. walsbyi TFEα (ERG94676), H. volcanii TFEα (ELK55987), H. sapiens C39 (EAX10240), S. cerevisiae C34 (P32910), S. solfataricus TFEβ (AAK41220), H. salinarum TFEβ (WP_010902769), H. walsbyi TFEβ (ERG96516), H. volcanii TFEβ (ADE03923). The secondary structure of the H. sapiens TFIIEα ZR domain is based on Okuda et al. (43).