Engineered protein switches for exogenous control of gene expression.
Allosteric Site
Animals
Biochemical Phenomena
Biosensing Techniques
/ methods
DNA
/ chemistry
Dimerization
Gene Expression
Gene Expression Regulation
Gene Regulatory Networks
Genetic Engineering
Humans
Mice
Mutagenesis
Mutation
Protein Domains
Protein Engineering
/ methods
Proteins
/ genetics
Signal Transduction
Substrate Specificity
Synthetic Biology
Transcription Factors
/ metabolism
protein engineering
protein switches
transcription factors
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
30 10 2020
30 10 2020
Historique:
received:
21
07
2020
revised:
28
09
2020
accepted:
30
09
2020
pubmed:
21
10
2020
medline:
10
8
2021
entrez:
20
10
2020
Statut:
ppublish
Résumé
There is an ongoing need in the synthetic biology community for novel ways to regulate gene expression. Protein switches, which sense biological inputs and respond with functional outputs, represent one way to meet this need. Despite the fact that there is already a large pool of transcription factors and signaling proteins available, the pool of existing switches lacks the substrate specificities and activities required for certain applications. Therefore, a large number of techniques have been applied to engineer switches with novel properties. Here we discuss some of these techniques by broadly organizing them into three approaches. We show how novel switches can be created through mutagenesis, domain swapping, or domain insertion. We then briefly discuss their use as biosensors and in complex genetic circuits.
Identifiants
pubmed: 33079167
pii: 226712
doi: 10.1042/BST20200441
doi:
Substances chimiques
Proteins
0
Transcription Factors
0
DNA
9007-49-2
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2205-2212Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM080189
Pays : United States
Informations de copyright
© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.