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Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii

机译:火山嗜血杆菌中的泛素样小古细菌修饰蛋白(SAMP)

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摘要

Archaea, one of three major evolutionary lineages of life, encode proteasomes highly related to those of eukaryotes. In contrast, archaeal ubiquitin-like proteins are less conserved and not known to function in protein conjugation. This has complicated our understanding of the origins of ubiquitination and its connection to proteasomes. Here we report two small archaeal modifier proteins, SAMP1 and SAMP2, with a β-grasp fold and carboxy-terminal diglycine motif similar to ubiquitin, that form protein conjugates in the archaeon Haloferax volcanii. The levels of SAMP-conjugates were altered by nitrogen-limitation and proteasomal gene knockout and spanned various functions including components of the Urm1 pathway. LC-MS/MS-based collision-induced dissociation demonstrated isopeptide bonds between the C-terminal glycine of SAMP2 and the ε-amino group of lysines from a number of protein targets and Lys 58 of SAMP2 itself, revealing poly-SAMP chains. The widespread distribution and diversity of pathways modified by SAMPylation suggest that this type of protein conjugation is central to the archaeal lineage.
机译:古细菌是生命的三个主要进化谱系之一,编码的蛋白酶体与真核生物高度相关。相反,古细菌类泛素蛋白保守性较低,并且不知道其在蛋白结合中的功能。这使我们对泛素化的起源及其与蛋白酶体的联系的理解变得复杂。在这里,我们报告了两个小的古细菌修饰蛋白,SAMP1和SAMP2,它们具有类似于泛素的β抓握折叠和羧基末端二甘氨酸基序,它们在古细菌Haloferax volcanii中形成蛋白质结合物。氮限制和蛋白酶体基因敲除改变了SAMP结合物的水平,并跨越了包括Urm1途径成分在内的各种功能。基于LC-MS / MS的碰撞诱导解离显示了SAMP2的C末端甘氨酸与来自许多蛋白质靶标的赖氨酸的ε-氨基和SAMP2本身的Lys 58之间的异肽键,揭示了多SAMP链。 SAMPylation修饰的途径的广泛分布和多样性表明,这种蛋白质偶联是古菌谱系的核心。

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  • 来源
    《Nature》 |2010年第7277期|54-60|共7页
  • 作者单位

    Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA;

    Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA;

    Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA;

    Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA;

    Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA;

    Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA;

    Department of Biology and Interdisciplinary Center for Biotechnological Research, University of Florida, Gainesville, Florida 32611, USA;

    Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA;

    Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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  • 正文语种 eng
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