| ○種別 (必須): | □ | 学術論文 (審査論文)
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| ○言語 (必須): | □ | 英語
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| ○招待 (推奨): |
| ○審査 (推奨): |
| ○カテゴリ (推奨): | □ | 研究
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| ○共著種別 (推奨): |
| ○学究種別 (推奨): |
| ○組織 (推奨): | 1. | 徳島大学.ゲノム機能研究センター (〜2008年3月31日/->組織[徳島大学.疾患プロテオゲノム研究センター])
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| 2. | 徳島大学.疾患プロテオゲノム研究センター (2008年4月1日〜2016年3月31日/->組織[徳島大学.先端酵素学研究所.プロテオゲノム研究領域])
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| ○著者 (必須): | 1. | (英) Iwahashi Akihiro (日) (読)
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| 2. | (英) Ishii Aoi (日) (読)
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| 3. | 山﨑 尚志 ([徳島大学.大学院医歯薬学研究部.薬学域.薬科学部門.生命薬学系.薬物治療学])
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| 4. | (英) Hashimoto Mutsuru (日) (読)
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| 5. | (英) Okura Kazuto (日) (読)
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| 6. | 片岡 正俊
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| 7. | 真島 英司 (アプロサイエンス)
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| 8. | 寺田 弘 ([東京理科大学])
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| 9. | 篠原 康雄 ([徳島大学.先端酵素学研究所.基幹研究部門])
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| ○題名 (必須): | □ | (英) Functionally important conserved length of C-terminal regions of yeast and bovine ADP/ATP carriers, identified by deletion mutants studies, and water accessibility of the amino acids at the C-terminal region of the yeast carrier. (日)
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| ○副題 (任意): |
| ○要約 (任意): | □ | (英) Comparison of the amino acid sequence of yeast type 2 ADP/ATP carrier (yAAC2) with that of bovine type 1 AAC (bAAC1) revealed that the N- and C-terminus of yAAC2 are 15- and 6-amino acids longer, respectively, than those of bAAC1. In the present study, we focused on the difference in the C-terminal region between yAAC2 and bAAC1. Deletion of first six residues of C-terminus of yAAC did not markedly affect the function of yAAC2; however, further deletion of 1 amino acid (7th amino acid from the C-terminus) destroyed its function. On the contrary, deletion of the first amino acid residue of the C-terminus of bAAC1 caused failure of its functional expression in yeast mitochondria. Based on these results, we concluded that the 6-amino acid residue extension of the C-terminus of yAAC2 was not necessary for the function of this carrier and that the remainder of the C-terminal region of yAAC2, having a length conserved with that of bAAC1, is important for the transport function of AACs. We next prepared various single-Cys mutants in which each of 32 residues in the C-terminus of yAAC2 was replaced by a Cys residue. Since all mutants were successfully expressed in yeast mitochondria, we examined the reactivity of these cysteine residues with the membrane-impermeable sulfhydryl reagent eosin 5-maleimide (EMA). As a result, all cysteine residues that replaced the 9 continuous amino acids in Met310-Lys318 showed high reactivity with EMA regardless of the presence of carboxyatractyloside or bongkrekic acid; and so this region was concluded to be exposed to the water-accessible environment. Furthermore, based on the reactivities of cysteine residues that replaced amino acids in the sixth transmembrane segment, the probable structural features of the C-terminal region of this carrier in the presence of bongkrekic acid were discussed. (日)
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| ○キーワード (推奨): | 1. | (英) Amino Acid Sequence (日) (読)
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| 2. | (英) Animals (日) (読)
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| 3. | (英) Bongkrekic Acid (日) (読)
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| 4. | (英) Cattle (日) (読)
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| 5. | (英) Eosine Yellowish-(YS) (日) (読)
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| 6. | (英) Gene Deletion (日) (読)
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| 7. | (英) Mitochondrial ADP, ATP Translocases (日) (読)
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| 8. | (英) Molecular Sequence Data (日) (読)
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| 9. | (英) Protein Conformation (日) (読)
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| 10. | (英) Saccharomyces cerevisiae Proteins (日) (読)
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| 11. | (英) Sequence Alignment (日) (読)
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| 12. | (英) Transformation, Genetic (日) (読)
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| ○発行所 (推奨): | □ | Elsevier (->組織[Elsevier Science])
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| ○誌名 (必須): | □ | Mitochondrion (Mitochondria Research Society)
(pISSN: 1567-7249, eISSN: 1872-8278)
| ○ISSN (任意): | □ | 1567-7249
ISSN: 1567-7249
(pISSN: 1567-7249, eISSN: 1872-8278) Title: MitochondrionTitle(ISO): MitochondrionPublisher: Elsevier BV (NLM Catalog)
(Scopus)
(CrossRef)
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| ○巻 (必須): | □ | 8
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| ○号 (必須): | □ | 2
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| ○頁 (必須): | □ | 196 204
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| ○都市 (任意): | □ | アムステルダム (Amsterdam/[オランダ王国])
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| ○年月日 (必須): | □ | 西暦 2008年 3月 初日 (平成 20年 3月 初日)
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| ○URL (任意): |
| ○DOI (任意): | □ | 10.1016/j.mito.2008.01.004 (→Scopusで検索)
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| ○PMID (任意): | □ | 18313366 (→Scopusで検索)
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| ○備考 (任意): | 1. | (英) Article.Affiliation: Institute for Genome Research, University of Tokushima, Kuramotocho-3, Tokushima 770-8503, Japan. (日)
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| 2. | (英) Article.PublicationTypeList.PublicationType: Comparative Study (日)
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| 3. | (英) Article.PublicationTypeList.PublicationType: Journal Article (日)
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