- EMDB-19077: Cryo-EM structure of P. urativorans 70S ribosome in complex with ... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-19077
タイトル
Cryo-EM structure of P. urativorans 70S ribosome in complex with hibernation factor Balon and EF-Tu(GDP) (structure 3).
マップデータ
試料
複合体: Ribosomes isolated from ice-treated cultures of Psychrobacter urativorans.
タンパク質・ペプチド: x 52種
RNA: x 3種
リガンド: x 3種
キーワード
Ribosome / Hibernation factor / Dormancy / Balon
機能・相同性
機能・相同性情報
guanosine tetraphosphate binding / translation elongation factor activity / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity ...guanosine tetraphosphate binding / translation elongation factor activity / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / GTPase activity / mRNA binding / GTP binding / RNA binding / cytosol / cytoplasm 類似検索 - 分子機能
Bacterial archaeo-eukaryotic release factor family 3 / Bacterial archaeo-eukaryotic release factor family 3 / Ribosomal protein L31 type B / Translation elongation factor EFTu/EF1A, C-terminal / Translation elongation factor EFTu/EF1A, bacterial/organelle / Ribosomal protein L7/L12, oligomerisation / Elongation factor Tu, domain 2 / Ribosomal protein L7/L12, oligomerisation domain superfamily / Elongation factor Tu (EF-Tu), GTP-binding domain / Ribosomal protein L7/L12 dimerisation domain ...Bacterial archaeo-eukaryotic release factor family 3 / Bacterial archaeo-eukaryotic release factor family 3 / Ribosomal protein L31 type B / Translation elongation factor EFTu/EF1A, C-terminal / Translation elongation factor EFTu/EF1A, bacterial/organelle / Ribosomal protein L7/L12, oligomerisation / Elongation factor Tu, domain 2 / Ribosomal protein L7/L12, oligomerisation domain superfamily / Elongation factor Tu (EF-Tu), GTP-binding domain / Ribosomal protein L7/L12 dimerisation domain / Ribosomal protein L7/L12 / Ribosomal protein L7/L12, C-terminal / Ribosomal protein L7/L12 C-terminal domain / : / Elongation factor Tu C-terminal domain / Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Ribosomal protein L25, long-form / Ribosomal protein L25, beta domain / Ribosomal protein L25, C-terminal / Ribosomal protein TL5, C-terminal domain / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation elongation factor EFTu-like, domain 2 / Ribosomal protein S21, conserved site / Ribosomal protein S21 signature. / Ribosomal protein L25, short-form / Ribosomal protein S14, bacterial/plastid / Elongation factor Tu domain 2 / Ribosomal protein S21 superfamily / Ribosomal protein S21 / Ribosomal protein S16, conserved site / Ribosomal protein S16 signature. / Ribosomal protein S21 / Ribosomal protein L31 signature. / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Ribosomal protein L31 / Ribosomal protein L31 superfamily / Ribosomal protein L31 / : / Ribosomal protein L21, conserved site / Ribosomal protein L21 signature. / Ribosomal protein L16 signature 1. / : / Ribosomal protein L6, conserved site / Ribosomal protein L6 signature 1. / Ribosomal protein L16, conserved site / Ribosomal protein L16 signature 2. / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal protein L17 signature. / Ribosomal L25p family / Ribosomal protein L25 / Ribosomal protein L36 signature. / Ribosomal protein L28/L24 superfamily / Ribosomal protein L25/Gln-tRNA synthetase, N-terminal / Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily / Ribosomal protein L32p, bacterial type / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal / Ribosomal protein L9, N-terminal domain / : / Ribosomal protein L28 / Ribosomal protein L35, conserved site / Ribosomal protein L35 signature. / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L5, bacterial-type / Ribosomal protein L18, bacterial-type / Ribosomal protein L6, bacterial-type / Ribosomal protein L9/RNase H1, N-terminal / Ribosomal protein L19, conserved site / Ribosomal protein L19 signature. / Ribosomal protein S3, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S6 signature. / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein L36 / Ribosomal protein L36 superfamily / Ribosomal protein L36 / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S11, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein L20 signature. / Ribosomal protein S9, bacterial/plastid / Ribosomal protein L27, conserved site / Ribosomal protein L27 signature. / Ribosomal protein S4, bacterial-type / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type 類似検索 - ドメイン・相同性
Small ribosomal subunit protein uS5 / Large ribosomal subunit protein uL16 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS14 / Large ribosomal subunit protein uL2 / Methyl-accepting chemotaxis protein / Large ribosomal subunit protein bL9 / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein uL30 ...Small ribosomal subunit protein uS5 / Large ribosomal subunit protein uL16 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS14 / Large ribosomal subunit protein uL2 / Methyl-accepting chemotaxis protein / Large ribosomal subunit protein bL9 / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein uL30 / Large ribosomal subunit protein uL22 / Large ribosomal subunit protein bL33 / Large ribosomal subunit protein bL12 / Large ribosomal subunit protein bL31B / Small ribosomal subunit protein bS21 / Large ribosomal subunit protein uL5 / Large ribosomal subunit protein uL3 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein bS20 / Small ribosomal subunit protein uS9 / Large ribosomal subunit protein uL15 / Small ribosomal subunit protein uS3 / Large ribosomal subunit protein bL28 / Large ribosomal subunit protein uL13 / Large ribosomal subunit protein uL29 / Small ribosomal subunit protein uS4 / Large ribosomal subunit protein uL24 / Small ribosomal subunit protein uS10 / Large ribosomal subunit protein bL34 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein uS2 / Large ribosomal subunit protein bL27 / Large ribosomal subunit protein uL18 / Small ribosomal subunit protein uS19 / Large ribosomal subunit protein bL19 / Large ribosomal subunit protein bL36 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein uS12 / Large ribosomal subunit protein bL35 / Elongation factor Tu / Large ribosomal subunit protein bL17 / Small ribosomal subunit protein uS8 / Large ribosomal subunit protein uL4 / Small ribosomal subunit protein bS6 / Large ribosomal subunit protein bL25 / Large ribosomal subunit protein uL23 / Small ribosomal subunit protein uS13 / Large ribosomal subunit protein bL20 / Large ribosomal subunit protein uL14 / Small ribosomal subunit protein bS18 / Large ribosomal subunit protein uL6 / Large ribosomal subunit protein bL21 類似検索 - 構成要素
ジャーナル: Nature / 年: 2024 タイトル: A new family of bacterial ribosome hibernation factors. 著者: Karla Helena-Bueno / Mariia Yu Rybak / Chinenye L Ekemezie / Rudi Sullivan / Charlotte R Brown / Charlotte Dingwall / Arnaud Baslé / Claudia Schneider / James P R Connolly / James N Blaza / ...著者: Karla Helena-Bueno / Mariia Yu Rybak / Chinenye L Ekemezie / Rudi Sullivan / Charlotte R Brown / Charlotte Dingwall / Arnaud Baslé / Claudia Schneider / James P R Connolly / James N Blaza / Bálint Csörgő / Patrick J Moynihan / Matthieu G Gagnon / Chris H Hill / Sergey V Melnikov / 要旨: To conserve energy during starvation and stress, many organisms use hibernation factor proteins to inhibit protein synthesis and protect their ribosomes from damage. In bacteria, two families of ...To conserve energy during starvation and stress, many organisms use hibernation factor proteins to inhibit protein synthesis and protect their ribosomes from damage. In bacteria, two families of hibernation factors have been described, but the low conservation of these proteins and the huge diversity of species, habitats and environmental stressors have confounded their discovery. Here, by combining cryogenic electron microscopy, genetics and biochemistry, we identify Balon, a new hibernation factor in the cold-adapted bacterium Psychrobacter urativorans. We show that Balon is a distant homologue of the archaeo-eukaryotic translation factor aeRF1 and is found in 20% of representative bacteria. During cold shock or stationary phase, Balon occupies the ribosomal A site in both vacant and actively translating ribosomes in complex with EF-Tu, highlighting an unexpected role for EF-Tu in the cellular stress response. Unlike typical A-site substrates, Balon binds to ribosomes in an mRNA-independent manner, initiating a new mode of ribosome hibernation that can commence while ribosomes are still engaged in protein synthesis. Our work suggests that Balon-EF-Tu-regulated ribosome hibernation is a ubiquitous bacterial stress-response mechanism, and we demonstrate that putative Balon homologues in Mycobacteria bind to ribosomes in a similar fashion. This finding calls for a revision of the current model of ribosome hibernation inferred from common model organisms and holds numerous implications for how we understand and study ribosome hibernation.
名称: 5S rRNA / タイプ: rna / ID: 11 詳細: Compared to reference sequence, it contains an insertion between bases 84 and 85 (an additional U) and a variant C88A コピー数: 1