徳島大学 教育・研究者情報データベース(EDB)

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])
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])

1. (英) Iwahashi Akihiro

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2. (英) Ishii Aoi

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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.創薬科学系.衛生薬学]/[徳島大学.薬学部.創製薬科学科.創薬学講座.衛生薬学]/[徳島大学.薬学研究科.創薬科学専攻])

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4. (英) Hashimoto Mutsuru

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5. (英) Okura Kazuto

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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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(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.

(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.

1. (英) Amino Acid Sequence
2. (英) Animals
3. (英) Bongkrekic Acid
4. (英) Cattle
5. (英) Eosine Yellowish-(YS)
6. (英) Gene Deletion
7. (英) Mitochondrial ADP, ATP Translocases
8. (英) Molecular Sequence Data
9. (英) Protein Conformation
10. (英) Saccharomyces cerevisiae Proteins
11. (英) Sequence Alignment
12. (英) Transformation, Genetic

1. (英) Article.Affiliation: Institute for Genome Research, University of Tokushima, Kuramotocho-3, Tokushima 770-8503, Japan.

2. (英) Article.PublicationTypeList.PublicationType: Comparative Study

3. (英) Article.PublicationTypeList.PublicationType: Journal Article