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Structural Basis for YjbH Adaptor-Mediated Recognition of Transcription Factor Spx

Awad, Wael LU ; Al-Eryani, Yusra LU ; Ekström, Simon LU ; Logan, Derek T. LU and von Wachenfeldt, Claes LU (2019) In Structure 27(6). p.6-936
Abstract

YjbH is a bacterial adaptor protein required for efficient proteolysis of the RNA polymerase-binding transcription factor Spx by the ClpXP protease. We report the structure of YjbH in complex with Spx. YjbH comprises a DsbA-like thioredoxin domain connected via a linker to a C-terminal domain reminiscent of the winged helix-turn-helix fold. The interaction between YjbH and Spx involves a large surface area. Binding to YjbH stabilizes the C-terminal ClpX recognition region of Spx. We show that mutation of critical YjbH contact residues abrogates Spx recognition. Small-angle X-ray scattering and hydrogen-deuterium exchange mass spectrometry analyses determined the existence of a stable heterodimeric complex in solution and provide... (More)

YjbH is a bacterial adaptor protein required for efficient proteolysis of the RNA polymerase-binding transcription factor Spx by the ClpXP protease. We report the structure of YjbH in complex with Spx. YjbH comprises a DsbA-like thioredoxin domain connected via a linker to a C-terminal domain reminiscent of the winged helix-turn-helix fold. The interaction between YjbH and Spx involves a large surface area. Binding to YjbH stabilizes the C-terminal ClpX recognition region of Spx. We show that mutation of critical YjbH contact residues abrogates Spx recognition. Small-angle X-ray scattering and hydrogen-deuterium exchange mass spectrometry analyses determined the existence of a stable heterodimeric complex in solution and provide evidence that binding of Spx to YjbH reduces the overall conformational flexibility of Spx. Our findings provide insights into the molecular basis for Spx recognition and suggest a model for how YjbH stabilizes Spx and displays the C terminus of Spx for engagement by ClpXP. Awad et al. determined the crystal structure of the ClpXP adaptor protein YjbH in complex with the transcription factor Spx. Structural dynamics of the complex were investigated by hydrogen-deuterium exchange mass spectrometry. The insights provided in this work add molecular details to the recognition of Spx by YjbH.

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Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
adaptor protein, ClpXP, proteolysis, Spx, stress response, YjbH
in
Structure
volume
27
issue
6
pages
6 - 936
publisher
Cell Press
external identifiers
  • scopus:85066242557
ISSN
0969-2126
DOI
10.1016/j.str.2019.03.009
language
English
LU publication?
yes
id
6c0213ce-eaaa-481f-b023-8b51743c06e1
date added to LUP
2019-06-11 11:05:06
date last changed
2019-10-15 07:07:32
@article{6c0213ce-eaaa-481f-b023-8b51743c06e1,
  abstract     = {<p>YjbH is a bacterial adaptor protein required for efficient proteolysis of the RNA polymerase-binding transcription factor Spx by the ClpXP protease. We report the structure of YjbH in complex with Spx. YjbH comprises a DsbA-like thioredoxin domain connected via a linker to a C-terminal domain reminiscent of the winged helix-turn-helix fold. The interaction between YjbH and Spx involves a large surface area. Binding to YjbH stabilizes the C-terminal ClpX recognition region of Spx. We show that mutation of critical YjbH contact residues abrogates Spx recognition. Small-angle X-ray scattering and hydrogen-deuterium exchange mass spectrometry analyses determined the existence of a stable heterodimeric complex in solution and provide evidence that binding of Spx to YjbH reduces the overall conformational flexibility of Spx. Our findings provide insights into the molecular basis for Spx recognition and suggest a model for how YjbH stabilizes Spx and displays the C terminus of Spx for engagement by ClpXP. Awad et al. determined the crystal structure of the ClpXP adaptor protein YjbH in complex with the transcription factor Spx. Structural dynamics of the complex were investigated by hydrogen-deuterium exchange mass spectrometry. The insights provided in this work add molecular details to the recognition of Spx by YjbH.</p>},
  author       = {Awad, Wael and Al-Eryani, Yusra and Ekström, Simon and Logan, Derek T. and von Wachenfeldt, Claes},
  issn         = {0969-2126},
  keyword      = {adaptor protein,ClpXP,proteolysis,Spx,stress response,YjbH},
  language     = {eng},
  number       = {6},
  pages        = {6--936},
  publisher    = {Cell Press},
  series       = {Structure},
  title        = {Structural Basis for YjbH Adaptor-Mediated Recognition of Transcription Factor Spx},
  url          = {http://dx.doi.org/10.1016/j.str.2019.03.009},
  volume       = {27},
  year         = {2019},
}