Suppr超能文献

在海栖假交替单胞菌 TAC125 中开发高拷贝数质粒。

Development of high-copy number plasmids in Pseudoalteromonas haloplanktis TAC125.

机构信息

Department of Chemical Sciences, Federico II University of Naples, Complesso Universitario Monte S.- Angelo, Via Cintia, 80126, Naples, Italy.

Istituto Nazionale di Oceanografia e di Geofisica Sperimentale, Oceanography Division - OGS, Trieste, Italy.

出版信息

Appl Microbiol Biotechnol. 2023 Apr;107(7-8):2469-2481. doi: 10.1007/s00253-023-12448-w. Epub 2023 Mar 13.

Abstract

The Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 (PhTAC125) is considered an interesting alternative host for the recombinant protein production, that can be explored when the conventional bacterial expression systems fail. Indeed, the manufacture of all the difficult-to-express proteins produced so far in this bacterial platform gave back soluble and active products. Despite these promising results, the low yield of recombinant protein production achieved is hampering the wider and industrial exploitation of this psychrophilic cell factory. All the expression plasmids developed so far in PhTAC125 are based on the origin of replication of the endogenous pMtBL plasmid and are maintained at a very low copy number. In this work, we set up an experimental strategy to select mutated OriR sequences endowed with the ability to establish recombinant plasmids at higher multiplicity per cell. The solution to this major production bottleneck was achieved by the construction of a library of psychrophilic vectors, each containing a randomly mutated version of pMtBL OriR, and its screening by fluorescence-activated cell sorting (FACS). The selected clones allowed the identification of mutated OriR sequences effective in enhancing the plasmid copy number of approximately two orders of magnitude, and the production of the recombinant green fluorescent protein was increased up to twenty times approximately. Moreover, the molecular characterization of the different mutant OriR sequences allowed us to suggest some preliminary clues on the pMtBL replication mechanism that deserve to be further investigated in the future. KEY POINTS: • Setup of an electroporation procedure for Pseudoalteromonas haloplanktis TAC125. • Two order of magnitude improvement of OriR-derived psychrophilic expression systems. • Almost twenty times enhancement in Green fluorescent protein production.

摘要

南极细菌假交替单胞菌 TAC125(PhTAC125)被认为是一种有趣的重组蛋白生产替代宿主,当传统的细菌表达系统失败时,可以探索这种替代宿主。事实上,迄今为止在该细菌平台上生产的所有难以表达的蛋白质都产生了可溶性和活性产物。尽管取得了这些有希望的结果,但重组蛋白生产的低产量仍阻碍了这种嗜冷细胞工厂的更广泛和工业开发。迄今为止在 PhTAC125 中开发的所有表达质粒都基于内源性 pMtBL 质粒的复制起点,并且以非常低的拷贝数维持。在这项工作中,我们建立了一种实验策略,以选择具有在每个细胞中建立更高重组质粒倍数的能力的突变 OriR 序列。通过构建包含 pMtBL OriR 随机突变版本的嗜冷载体文库,并通过荧光激活细胞分选(FACS)对其进行筛选,解决了这个主要的生产瓶颈问题。所选克隆允许鉴定出突变 OriR 序列,这些序列有效地将质粒拷贝数提高了大约两个数量级,并且重组绿色荧光蛋白的产量增加了大约二十倍。此外,对不同突变 OriR 序列的分子特征分析使我们能够提出一些关于 pMtBL 复制机制的初步线索,这些线索值得在未来进一步研究。关键点:• 为假交替单胞菌 TAC125 建立电穿孔程序。• OriR 衍生的嗜冷表达系统提高了两个数量级。• 绿色荧光蛋白产量提高了近二十倍。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cbbc/10033558/6d239f1902c7/253_2023_12448_Fig1_HTML.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验