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Analysis on interaction between archaeal ribosomal stalk proteins and translation elongation factors
http://hdl.handle.net/10191/47460
http://hdl.handle.net/10191/4746016f024c4-2174-497c-b424-0ab383cbcd1e
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本文 (1.2 MB)
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要旨 (155.3 kB)
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| Item type | 学位論文 / Thesis or Dissertation(1) | |||||
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| 公開日 | 2017-05-12 | |||||
| タイトル | ||||||
| タイトル | Analysis on interaction between archaeal ribosomal stalk proteins and translation elongation factors | |||||
| タイトル | ||||||
| タイトル | Analysis on interaction between archaeal ribosomal stalk proteins and translation elongation factors | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源 | http://purl.org/coar/resource_type/c_46ec | |||||
| タイプ | thesis | |||||
| その他のタイトル | ||||||
| その他のタイトル | 古細菌リボソームストークタンパク質と翻訳伸長因子間の相互作用解析 | |||||
| 著者 |
Honda, Takayoshi
× Honda, Takayoshi |
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| 著者別名 | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 51100 | |||||
| 姓名 | 本田, 貴嘉 | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The translation elongation cycle is main event in protein synthesis and this cycle requires alternatively binding of two elongation factors. The multiple copies of the flexible ribosomal stalk protein interact directly with the elongation factors and play a crucial role in these processes. Archaeal ribosomes have three stalk homodimers (aP1)_2 that constitute a heptameric complex with the anchor protein aP0. I investigated the factor binding ability of aP1 proteins assembled onto aP0, by gel-retardation assays. The isolated aP0(aP1)_2(aP1)_2(aP1)_2 complex, as well as the form bound to the E. coli 50S core, as a hybrid 50S particle, interacted strongly with elongation factor aEF2, but weakly with aEF1A. These interactions were disrupted by a point mutation, F107S, at the C-terminus of aP1. To examine the ability of each copy of aP0-associated aP1 to bind to elongation factors, I constructed aP0•aP1 variant trimers, composed of an aP0 mutant and a single (aP1)_2 dimer. Biochemical and quantitative analyses revealed that the resultant three trimers, aP0(aP1)_2＾I, aP0(aP1)_2＾II, and aP0(aP1)_2＾III, individually bound two molecules of aEF2, suggesting that each copy of the aP1 C-terminal region in the aP0•aP1 trimers can bind tightly to aEF2. Interestingly, the unstable binding of aEF1A to each of the three aP0•aP1 trimers was remarkably stabilized in the presence of aEF2. This stabilization of the aEF1A binding to the stalk complex may contribute to promotion of an efficient translation elongation cycle. | |||||
| 内容記述 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 学位の種類: 博士（理学）. 報告番号: 甲第4322号. 学位記番号: 新大院博（理）甲第421号. 学位授与年月日: 平成29年3月23日 | |||||
| 書誌情報 | 発行日 2017-03-23 | |||||
| 出版者 | ||||||
| 出版者 | 新潟大学 | |||||
| 著者版フラグ | ||||||
| 値 | ETD | |||||
| 学位名 | ||||||
| 学位名 | 博士（理学） | |||||
| 学位授与機関 | ||||||
| 学位授与機関名 | 新潟大学 | |||||
| 学位授与年月日 | ||||||
| 学位授与年月日 | 2017-03-23 | |||||
| 学位授与番号 | ||||||
| 学位授与番号 | 13101甲第4322号 | |||||
| 学位記番号 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 新大院博（理）甲第421号 | |||||
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Cite as
Honda, Takayoshi, 2017, Analysis on interaction between archaeal ribosomal stalk proteins and translation elongation factors: 新潟大学.
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