DSpace Repository

Enhancement of lysine biosynthesis confers high-temperature stress tolerance to Escherichia coli cells

Show simple item record

dc.contributor.author Isogai, Shota en
dc.contributor.author Takagi, Hiroshi en
dc.date.accessioned 2021-12-08T01:43:56Z en
dc.date.available 2021-12-08T01:43:56Z en
dc.date.issued 2021-08-29 en
dc.identifier.uri http://hdl.handle.net/10061/14572 en
dc.description.abstract Lysine, a nutritionally important amino acid, is involved in adaptation and tolerance to environmental stresses in various organisms. Previous studies reported that lysine accumulation occurs in response to stress and that lysine supplementation enhances stress tolerance; however, the effect of lysine biosynthesis enhancement on stress tolerance has yet to be elucidated. In this study, we confirmed that lysine supplementation to the culture medium increased intracellular lysine content and improved cell growth of Escherichia coli at high temperature (42.5 °C). Lysine-overproducing strains were then isolated from the lysine analogue S-adenosylmethionine-resistant mutants by conventional mutagenesis and exhibited higher tolerance to high-temperature stress than the wild-type strain. We identified novel amino acid substitutions Gly474Asp and Cys554Tyr on ThrA, a bifunctional aspartate kinase/homoserine dehydrogenase (AK/HSDH), in the lysine-overproducing mutants. Interestingly, the Gly474Asp and Cys554Tyr variants of ThrA induced lysine accumulation and conferred high-temperature stress tolerance to E. coli cells. Enzymatic analysis revealed that the Gly474Asp substitution in ThrA reduced HSDH activity, suggesting that the intracellular level of aspartate semialdehyde, which is a substrate for HSDH and an intermediate for lysine biosynthesis, is elevated by the loss of HSDH activity and converted to lysine in E. coli. The present study demonstrated that both lysine supplementation and lysine biosynthesis enhancement improved the high-temperature stress tolerance of E. coli cells. Our findings suggest that lysine-overproducing strains have the potential as stress-tolerant microorganisms and can be applied to robust host cells for microbial production of useful compounds. ja
dc.language.iso en en
dc.publisher Springer en
dc.rights © 2021, The Author(s) This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. ja
dc.subject Escherichia coli en
dc.subject Lysine en
dc.subject ThrA en
dc.subject Aspartate kinase en
dc.subject Homoserine dehydrogenase en
dc.subject Stress tolerance en
dc.title Enhancement of lysine biosynthesis confers high-temperature stress tolerance to Escherichia coli cells en
dc.type.nii Journal Article en
dc.contributor.transcription イソガイ, ショウタ ja
dc.contributor.transcription タカギ, ヒロシ ja
dc.contributor.alternative 磯貝, 章太 ja
dc.contributor.alternative 高木, 博史 ja
dc.textversion publisher en
dc.identifier.eissn 1432-0614 en
dc.identifier.jtitle Applied Microbiology and Biotechnology en
dc.identifier.volume 105 en
dc.identifier.issue 18 en
dc.identifier.spage 6899 en
dc.identifier.epage 6908 en
dc.relation.doi 10.1007/s00253-021-11519-0 en
dc.identifier.NAIST-ID 74655085 en
dc.identifier.NAIST-ID 73290561 en
dc.relation.pmid 34455479 en
dc.relation.isIdenticalTo https://rd.springer.com/article/10.1007%2Fs00253-021-11519-0 en


Files in this item

This item appears in the following Collection(s)

Show simple item record

Search DSpace


Advanced Search

Browse

My Account