Karapanagioti Foteini, Obermaier Sebastian, Slotboom Dirk J, Poolman Bert
Department of Biochemistry, University of Groningen, The Netherlands.
FEBS Lett. 2025 Jun;599(11):1609-1621. doi: 10.1002/1873-3468.70044. Epub 2025 Apr 18.
The main mediators for the amino acid uptake in Saccharomyces cerevisiae are the permeases belonging to the yeast amino acid transporter family. Recently, we discovered that members of this family support growth on more amino acids than previously described. Here we study the substrate spectrum of Lyp1, the main transporter responsible for the uptake of lysine in yeast. We show that overexpressed Lyp1 supports growth on alanine, asparagine, leucine, methionine, phenylalanine, serine, and valine when these are provided as the sole source of nitrogen to a strain severely deficient for the uptake of amino acids. We show that alanine and serine compete with lysine for the common transport system, albeit with much lower affinity. Thus, Lyp1 has a much broader substrate spectrum than previously thought, which may be true for many amino acid transporters.
酿酒酵母中负责氨基酸摄取的主要介质是属于酵母氨基酸转运蛋白家族的通透酶。最近，我们发现该家族成员支持酵母在比先前描述的更多种类氨基酸上生长。在此，我们研究了Lyp1的底物谱，它是酵母中负责赖氨酸摄取的主要转运蛋白。我们发现，当将丙氨酸、天冬酰胺、亮氨酸、蛋氨酸、苯丙氨酸、丝氨酸和缬氨酸作为唯一氮源提供给一个严重缺乏氨基酸摄取能力的菌株时，过表达的Lyp1能支持该菌株生长。我们还发现，丙氨酸和丝氨酸与赖氨酸竞争共同的转运系统，尽管亲和力要低得多。因此，Lyp1的底物谱比先前认为的要广泛得多，这可能对许多氨基酸转运蛋白来说都是如此。
