一种由遗传漂移和基因组缩减形成的细菌内共生体的新型赖氨酸生物合成酶。

IF 4.5 3区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Protein Science Pub Date : 2024-07-01 DOI:10.1002/pro.5083
Jenna M Gilkes, Rebekah A Frampton, Amanda J Board, André O Hudson, Thomas G Price, Vanessa K Morris, Deborah L Crittenden, Andrew C Muscroft-Taylor, Campbell R Sheen, Grant R Smith, Renwick C J Dobson
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引用次数: 0

摘要

人们对种群瓶颈和基因组减少对酶功能的影响知之甚少。Candidatus Liberibacter solanacearum 是一种基因组减少的细菌,它通过垂直传播到受感染的牛皮蝉卵中--这种种群瓶颈造成了遗传漂移,预计会影响蛋白质的结构和功能。在这里,我们确定了Ca.L. solanacearum dihydrodipicolinate synthase (CLsoDHDPS)的功能,它催化二氨基丙二酸盐和赖氨酸生物合成过程中的承诺支点反应。我们证明,CLsoDHDPS 在 Ca.L.solanacearum中表达,而且在昆虫宿主体内的表达量比在植物体内增加了约2倍。CLsoDHDPS 的热稳定性降低,聚集倾向增加,这意味着突变破坏了酶的稳定性,但通过伴侣表达的增加和稳定的低聚物状态得到了补偿。CLsoDHDPS 采用三元复合动力学机制,这在迄今为止的 DHDPS 酶中是独一无二的,其催化能力异常低,但底物亲和力异常高。结构研究表明,CLsoDHDPS 的活性位点更加开放,丙酮酸和底物类似物琥珀酰半乳糖醛的结构显示,产物在结构上和能量上都不同,因此在这种情况下,进化产生了一种新的酶。我们的研究表明了基因组减少和基因漂移对必需酶功能的影响,并为细菌-宿主共同进化关系提供了启示。我们认为,具有内共生生活方式的细菌提供了大量有趣的酶,有助于了解酶的功能和/或为蛋白质工程提供信息。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A new lysine biosynthetic enzyme from a bacterial endosymbiont shaped by genetic drift and genome reduction.

The effect of population bottlenecks and genome reduction on enzyme function is poorly understood. Candidatus Liberibacter solanacearum is a bacterium with a reduced genome that is transmitted vertically to the egg of an infected psyllid-a population bottleneck that imposes genetic drift and is predicted to affect protein structure and function. Here, we define the function of Ca. L. solanacearum dihydrodipicolinate synthase (CLsoDHDPS), which catalyzes the committed branchpoint reaction in diaminopimelate and lysine biosynthesis. We demonstrate that CLsoDHDPS is expressed in Ca. L. solanacearum and expression is increased ~2-fold in the insect host compared to in planta. CLsoDHDPS has decreased thermal stability and increased aggregation propensity, implying mutations have destabilized the enzyme but are compensated for through elevated chaperone expression and a stabilized oligomeric state. CLsoDHDPS uses a ternary-complex kinetic mechanism, which is to date unique among DHDPS enzymes, has unusually low catalytic ability, but an unusually high substrate affinity. Structural studies demonstrate that the active site is more open, and the structure of CLsoDHDPS with both pyruvate and the substrate analogue succinic-semialdehyde reveals that the product is both structurally and energetically different and therefore evolution has in this case fashioned a new enzyme. Our study suggests the effects of genome reduction and genetic drift on the function of essential enzymes and provides insights on bacteria-host co-evolutionary associations. We propose that bacteria with endosymbiotic lifestyles present a rich vein of interesting enzymes useful for understanding enzyme function and/or informing protein engineering efforts.

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来源期刊
Protein Science
Protein Science 生物-生化与分子生物学
CiteScore
12.40
自引率
1.20%
发文量
246
审稿时长
1 months
期刊介绍: Protein Science, the flagship journal of The Protein Society, is a publication that focuses on advancing fundamental knowledge in the field of protein molecules. The journal welcomes original reports and review articles that contribute to our understanding of protein function, structure, folding, design, and evolution. Additionally, Protein Science encourages papers that explore the applications of protein science in various areas such as therapeutics, protein-based biomaterials, bionanotechnology, synthetic biology, and bioelectronics. The journal accepts manuscript submissions in any suitable format for review, with the requirement of converting the manuscript to journal-style format only upon acceptance for publication. Protein Science is indexed and abstracted in numerous databases, including the Agricultural & Environmental Science Database (ProQuest), Biological Science Database (ProQuest), CAS: Chemical Abstracts Service (ACS), Embase (Elsevier), Health & Medical Collection (ProQuest), Health Research Premium Collection (ProQuest), Materials Science & Engineering Database (ProQuest), MEDLINE/PubMed (NLM), Natural Science Collection (ProQuest), and SciTech Premium Collection (ProQuest).
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