Institute of Molecular Biosciences, Mahidol University, 25/25 Phuttamonthon 4 Road, Salaya, Phuttamonthon, Nakhon Pathom, 73170, Thailand.
Section of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, 9500 Gilman Drive (MC 0347), La Jolla, CA, 92093-0347, USA.
Sci Rep. 2019 Jan 22;9(1):278. doi: 10.1038/s41598-018-36719-z.
Recent work has found that many metabolic enzymes have the ability to polymerize in response to metabolic changes or environmental stress. This ability to polymerize is well conserved for the few metabolic enzyme paralogs that have been studied in yeast. Here we describe the first set of paralogs, Asn1p and Asn2p, that have differential assembly behavior. Asn1p and Asn2p both co-assemble into filaments in response to nutrient limitation. However, the ability of Asn2p to form filaments is strictly dependent on the presence of Asn1p. Using mutations that block enzyme activity but have differential effects on Asn1p polymerization, we have found that Asn1p polymers are unlikely to have acquired a moonlighting function. Together these results provide a novel system for understanding the regulation and evolution of metabolic enzyme polymerization.
最近的研究发现,许多代谢酶具有在代谢变化或环境压力下聚合的能力。在已研究过的少数几种酵母代谢酶的同工酶中,这种聚合能力得到了很好的保留。在这里,我们描述了第一组具有不同组装行为的同工酶,Asn1p 和 Asn2p。Asn1p 和 Asn2p 都能在营养限制的情况下共同组装成纤维。然而,Asn2p 形成纤维的能力严格依赖于 Asn1p 的存在。通过使用阻断酶活性但对 Asn1p 聚合有不同影响的突变,我们发现 Asn1p 聚合物不太可能获得兼职功能。这些结果共同为理解代谢酶聚合的调节和进化提供了一个新的系统。