Structure of radical-induced cell death1 hub domain reveals a common αα-scaffold for disorder in transcriptional networks
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Structure of radical-induced cell death1 hub domain reveals a common αα-scaffold for disorder in transcriptional networks. / Bugge, Katrine Østergaard; Staby, Lasse; Kemplen, Katherine Rosemary; O'Shea, Charlotte; Bendsen, Sidsel Krogh; Jensen, Mikael Kryger; Olsen, Johan Gotthardt; Skriver, Karen; Kragelund, Birthe Brandt.
In: Structure, Vol. 26, No. 5, 2018, p. 734-746.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Structure of radical-induced cell death1 hub domain reveals a common αα-scaffold for disorder in transcriptional networks
AU - Bugge, Katrine Østergaard
AU - Staby, Lasse
AU - Kemplen, Katherine Rosemary
AU - O'Shea, Charlotte
AU - Bendsen, Sidsel Krogh
AU - Jensen, Mikael Kryger
AU - Olsen, Johan Gotthardt
AU - Skriver, Karen
AU - Kragelund, Birthe Brandt
N1 - Copyright © 2018 Elsevier Ltd. All rights reserved.
PY - 2018
Y1 - 2018
N2 - Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversely, folded hub proteins may organize networks using disordered partners. In this work, the structure of the RST domain, a unique folded hub, is solved by nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, and its complex with a region of the transcription factor DREB2A is provided through data-driven HADDOCK modeling and mutagenesis analysis. The RST fold is unique, but similar structures are identified in the PAH (paired amphipathic helix), TAFH (TATA-box-associated factor homology), and NCBD (nuclear coactivator binding domain) domains. We designate them as a group the αα hubs, as they share an αα-hairpin super-secondary motif, which serves as an organizing platform for malleable helices of varying topology. This allows for partner adaptation, exclusion, and selection. Our findings provide valuable insights into structural features enabling signaling fidelity.
AB - Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversely, folded hub proteins may organize networks using disordered partners. In this work, the structure of the RST domain, a unique folded hub, is solved by nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, and its complex with a region of the transcription factor DREB2A is provided through data-driven HADDOCK modeling and mutagenesis analysis. The RST fold is unique, but similar structures are identified in the PAH (paired amphipathic helix), TAFH (TATA-box-associated factor homology), and NCBD (nuclear coactivator binding domain) domains. We designate them as a group the αα hubs, as they share an αα-hairpin super-secondary motif, which serves as an organizing platform for malleable helices of varying topology. This allows for partner adaptation, exclusion, and selection. Our findings provide valuable insights into structural features enabling signaling fidelity.
U2 - 10.1016/j.str.2018.03.013
DO - 10.1016/j.str.2018.03.013
M3 - Journal article
C2 - 29657132
VL - 26
SP - 734
EP - 746
JO - Structure
JF - Structure
SN - 0969-2126
IS - 5
ER -
ID: 200579231