Mueller-Cajar Oliver, Whitney Spencer M
Molecular Plant Physiology, Research School of Biological Sciences, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Photosynth Res. 2008 Oct-Dec;98(1-3):667-75. doi: 10.1007/s11120-008-9324-z. Epub 2008 Jul 15.
During the last decade the practice of laboratory-directed protein evolution has become firmly established as a versatile tool in biochemical research by enabling molecular evolution toward desirable phenotypes or detection of novel structure-function interactions. Applications of this technique in the field of photosynthesis research are still in their infancy, but recently first steps have been reported in the directed evolution of the CO(2)-fixing enzyme Rubisco and its helper protein Rubisco activase. Here we summarize directed protein evolution strategies and review the progressive advances that have been made to develop and apply suitable selection systems for screening mutant forms of these enzymes that improve the fitness of the host organism. The goal of increasing photosynthetic efficiency of plants by improving the kinetics of Rubisco has been a long-term goal scoring modest successes. We discuss how directed evolution methodologies may one day be able to circumvent the problems encountered during this venture.
在过去十年中，实验室导向的蛋白质进化实践已成为生化研究中的一种通用工具，它能够使分子朝着理想表型进化或检测新的结构 - 功能相互作用。该技术在光合作用研究领域的应用仍处于起步阶段，但最近已有报道称在固定二氧化碳的酶核酮糖 - 1,5 - 二磷酸羧化酶（Rubisco）及其辅助蛋白Rubisco活化酶的定向进化方面迈出了第一步。在此，我们总结了定向蛋白质进化策略，并回顾了在开发和应用合适的选择系统以筛选这些酶的突变形式从而提高宿主生物体适应性方面所取得的进展。通过改善Rubisco的动力学来提高植物光合效率这一长期目标已取得了一定成效。我们讨论了定向进化方法有朝一日如何能够规避在此过程中遇到的问题。
