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Fusion with heat-resistant obscure (Hero) proteins have the potential to improve the molecular property of recombinant proteins

Authors
  • Morimoto, Eri
  • Tsuboyama, Kotaro
  • Tomari, Yukihide
Type
Published Article
Journal
PLoS ONE
Publisher
Public Library of Science
Publication Date
Jun 17, 2022
Volume
17
Issue
6
Identifiers
DOI: 10.1371/journal.pone.0270097
PMID: 35714106
PMCID: PMC9205492
Source
PubMed Central
Disciplines
  • Medicine and Health Sciences
  • Neurology
  • Neurodegenerative Diseases
  • Motor Neuron Diseases
  • Amyotrophic Lateral Sclerosis
License
Unknown

Abstract

Although recombinant proteins are widely used in biotechnology and pharmaceutical industries, improving their solubility and stability is often a challenging issue. We recently discovered a class of highly unstructured heat-resistant obscure (Hero) proteins, which function to protect other “client” proteins in trans from various stresses in vitro and in vivo . Here, we show that fusion of Hero proteins in cis can enhance the molecular property of recombinant proteins. Fusion with Hero11 improved the otherwise challenging production of TAR DNA-binding protein of 43 kDa (TDP-43) in Escherichia coli . Moreover, fusing with Hero9 strongly protected the activity of firefly luciferase bearing destabilizing mutations against heat and other stress conditions. These data suggest that Hero proteins have the potential to be used as versatile stabilization tags for recombinant protein production.

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