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十二菌素是古菌黄素稳态中的关键因子。

Dodecin is the key player in flavin homeostasis of archaea.

作者信息

Grininger Martin, Staudt Heike, Johansson Patrik, Wachtveitl Josef, Oesterhelt Dieter

机构信息

Department of Membrane Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.

出版信息

J Biol Chem. 2009 May 8;284(19):13068-76. doi: 10.1074/jbc.M808063200. Epub 2009 Feb 17.

DOI:10.1074/jbc.M808063200
PMID:19224924
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2676039/
Abstract

Flavins are employed to transform physical input into biological output signals. In this function, flavins catalyze a variety of light-induced reactions and redox processes. However, nature also provides flavoproteins with the ability to uncouple the mediation of signals. Such proteins are the riboflavin-binding proteins (RfBPs) with their function to store riboflavin for fast delivery of FMN and FAD. Here we present in vitro and in vivo data showing that the recently discovered archaeal dodecin is an RfBP, and we reveal that riboflavin storage is not restricted to eukaryotes. However, the function of the prokaryotic RfBP dodecin seems to be adapted to the requirement of a monocellular organism. While in eukaryotes RfBPs are involved in trafficking riboflavin, and dodecin is responsible for the flavin homeostasis of the cell. Although only 68 amino acids in length, dodecin is of high functional versatility in neutralizing riboflavin to protect the cellular environment from uncontrolled flavin reactivity. Besides the predominant ultrafast quenching of excited states, dodecin prevents light-induced riboflavin reactivity by the selective degradation of riboflavin to lumichrome. Coordinated with the high affinity for lumichrome, the directed degradation reaction is neutral to the cellular environment and provides an alternative pathway for suppressing uncontrolled riboflavin reactivity. Intriguingly, the different structural and functional properties of a homologous bacterial dodecin suggest that dodecin has different roles in different kingdoms of life.

摘要

黄素被用于将物理输入转化为生物输出信号。在这一功能中,黄素催化各种光诱导反应和氧化还原过程。然而,自然界也赋予了黄素蛋白解耦信号介导的能力。这类蛋白质就是核黄素结合蛋白(RfBPs),其功能是储存核黄素以便快速递送FMN和FAD。在此,我们展示了体外和体内数据,表明最近发现的古菌十二聚体蛋白是一种RfBP,并且我们揭示核黄素储存并不局限于真核生物。然而,原核生物的RfBP十二聚体蛋白的功能似乎是适应单细胞生物的需求。在真核生物中,RfBPs参与核黄素的运输,而十二聚体蛋白负责细胞的黄素稳态。尽管十二聚体蛋白仅有68个氨基酸长,但它在中和核黄素以保护细胞环境免受不受控制的黄素反应性影响方面具有高度的功能多样性。除了对激发态的主要超快猝灭作用外,十二聚体蛋白通过将核黄素选择性降解为光色素来防止光诱导的核黄素反应性。与对光色素的高亲和力相协调,定向降解反应对细胞环境是中性的,并提供了一条抑制不受控制的核黄素反应性的替代途径。有趣的是,同源细菌十二聚体蛋白的不同结构和功能特性表明,十二聚体蛋白在不同的生命王国中具有不同的作用。

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本文引用的文献

1
Crystal structures of NADH:FMN oxidoreductase (EmoB) at different stages of catalysis.催化不同阶段的NADH:FMN氧化还原酶(EmoB)的晶体结构。
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The dodecin from Thermus thermophilus, a bifunctional cofactor storage protein.嗜热栖热菌中的十二聚体蛋白,一种双功能辅因子储存蛋白。
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Donor-acceptor distance-dependence of photoinduced electron-transfer rate in flavoproteins.黄素蛋白中光诱导电子转移速率的供体-受体距离依赖性。
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BluB cannibalizes flavin to form the lower ligand of vitamin B12.BluB分解黄素以形成维生素B12的下部配体。
Nature. 2007 Mar 22;446(7134):449-53. doi: 10.1038/nature05611.
6
Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12.单酶将黄素单核苷酸还原酶(FMNH2)转化为5,6-二甲基苯并咪唑,即维生素B12的下侧配体。
Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2921-6. doi: 10.1073/pnas.0609270104. Epub 2007 Feb 14.
7
Dodecin sequesters FAD in closed conformation from the aqueous solution.十二菌素在封闭构象中从水溶液中螯合黄素腺嘌呤二核苷酸。
J Mol Biol. 2006 Dec 8;364(4):561-6. doi: 10.1016/j.jmb.2006.08.083. Epub 2006 Sep 5.
8
Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.嗜热栖热菌呼吸链复合体I亲水结构域的结构
Science. 2006 Mar 10;311(5766):1430-6. doi: 10.1126/science.1123809. Epub 2006 Feb 9.
9
Dodecins: a family of lumichrome binding proteins.核黄素结合蛋白:一类与核黄素结合的蛋白质。
J Mol Biol. 2006 Mar 31;357(3):842-57. doi: 10.1016/j.jmb.2005.12.072. Epub 2006 Jan 18.
10
MpcT is the transducer for membrane potential changes in Halobacterium salinarum.MpcT是盐生盐杆菌中膜电位变化的传感器。
Mol Microbiol. 2005 Mar;55(6):1681-94. doi: 10.1111/j.1365-2958.2005.04516.x.