Evidence map›Paper›PMID 42616204›Full record

ArticleBiotechnology letters2026

Regulation of N-terminal cleavage and splicing in mini-Ter DnaE-3 intein by E23G and R50Q mutations.

Xuhan Wei, Ying Lin

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Article in Biotechnology letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

2 authors.

Xuhan WeiCollege of Biological Science and Medical Engineering, Donghua University, Shanghai, 201620, People's Republic of China.
Ying LinCollege of Biological Science and Medical Engineering, Donghua University, Shanghai, 201620, People's Republic of China. liny@dhu.edu.cn.

Funding

National Natural Science Foundation of China No.31470836
6 · The paper itself

Abstract

backgroundAs a member of the DnaE intein family, Ter DnaE-3 (TE3) is limited by a relatively low splicing rate, significant undesired N-terminal cleavage reactions, and dependence on native exteins.

methodsBuilding on eight previously identified mutation sites from directed evolution, we employed site-directed mutagenesis to systematically investigate how these residues regulate wild-type mini-TE3 splicing and cleavage activities across various expression systems.

resultsIn the pKH kanamycin resistance system, the E23G mutation reduces N-cleavage propensity, which may be attributed to reduced steric hindrance and enhanced structural flexibility. Conversely, in both pKH and pMST systems, the R50Q mutation increases the accumulation of N-terminal cleavage products, suggesting that intein catalysis may be influenced by a distributed regulatory network rather than by isolated residues.

conclusionThese results suggest that the catalytic behavior of TE3 is governed not only by conserved catalytic cores and adjacent extein sequences but also by distal residues that modulate the intein structure. The discovery that R50Q enhances N-terminal cleavage provides a valuable tool for future protein engineering, particularly for optimizing intein-based protein purification and expressed protein ligation (EPL) technologies.

Indexed as

DNA Polymerase IIIInteinsProtein SplicingEscherichia coliMutagenesis, Site-DirectedMutationDNA Polymerase IIIDNA polymerase III, alpha subunitInteinN-terminal cleavageProtein splicingTer DnaE-3

Identifiers

PMID42616204

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