Frame-shifted proteins of a given gene retain the same function

Frameshift mutations are generally considered to be lethal because it could result in radical changes of the protein sequence behind. However, the protein of frameshift mutants of a type I toxin (ibsc) was found to be still toxic to bacteria, retaining the similar function as wild-type protein to ar...

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Bibliographic Details
Published in:Nucleic acids research 2020-05, Vol.48 (8), p.4396-4404
Main Authors: Huang, Xin, Chen, Rong, Sun, Meiling, Peng, Yan, Pu, Qinlin, Yuan, Yi, Chen, Gangyi, Dong, Juan, Du, Feng, Cui, Xin, Tang, Zhuo
Format: Article
Language:English
Subjects:
Molecular Biology
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Summary:Frameshift mutations are generally considered to be lethal because it could result in radical changes of the protein sequence behind. However, the protein of frameshift mutants of a type I toxin (ibsc) was found to be still toxic to bacteria, retaining the similar function as wild-type protein to arrest the cellular growth by impairing the membrane's integrity. Additionally, we have verified that this observation is not an individual event as the same phenomenon had been found in other toxins subsequently. After analyzing the coding sequence of these genes, we proposed a hypothesis to search this kind of hidden gene, through which a dihydrofolate reductase-encoding gene (dfrB3) was found out. Like the wild-type reductase, both +1 and -1 frame-shifted proteins of dfrB3 gene were also proved to catalyze the reduction of dihydrofolate to tetrahydrofolate by using NADPH.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkaa169