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UDP-GalNAc : Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) の構造活性相関 : GalNAc-T1のレクチン様ドメインの機能解析
http://hdl.handle.net/10965/464
http://hdl.handle.net/10965/46437b9d03a-ab7d-4498-ace2-045c93365912
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
AHSUSK_NSS_33_60.pdf (924.8 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-09-30 | |||||
| タイトル | ||||||
| タイトル | UDP-GalNAc : Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) の構造活性相関 : GalNAc-T1のレクチン様ドメインの機能解析 | |||||
| 言語 | ja | |||||
| タイトル | ||||||
| タイトル | Structure-function Relationship of UDP-GalNAc : Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) : Function of the Lectin Domain of GalNAc-T1 | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | ムチン型O-グリコシレーション，GalNAc 転移酵素，レクチン様ドメイン，構造活性相関，部位特異的変異 | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | mucin-type O-glycosylation | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | GalNAc-transferase | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | lectin domain | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | structurefunction relationship | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題Scheme | Other | |||||
| 主題 | site-directed mutagenesis | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | departmental bulletin paper | |||||
| 著者 |
天野, 麻理
× 天野, 麻理 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The initial step of mucin-type O-glycosylation is catalyzed by UDP-GalNAc : polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). GalNAc-transferases contain a lectin domain at the C-terminus, consisting of three tandem repeats (α, β, and γ). I have reevaluated the role of the GalNAc-T1 lectin domain in this study, because the putative lectin domain of this enzyme is reportedly not functional. Deletion of the lectin domain resulted in a complete loss of enzymatic activity. I found that GalNAc-T1 has two activities distinguished by their sensitivities to inhibition with free GalNAc; one activity is sensitive, the other is resistant. In my experiments, the former activity is represented by the O-glycosylation of apomucin, an acceptor that contains multiple glycosylation sites, and the latter by synthetic peptides that contain a single glycosylation site. Site-directed mutagenesis of the lectin domain selectively reduced the follow-up activity, and identified Asp444 in the α repeat as the most important site for GalNAc recognition. I also found that the β repeat recognizes GalNAc and is involved in glycosylation of acceptors with multiple glycosylation sites. These results indicate that the lectin domain of GalNAc-T1 has at least two functional repeats, allowing the possibility of multivalent interactions with GalNAc residues on the acceptor peptide during glycosylation. | |||||
| 書誌情報 |
京都産業大学論集. 自然科学系列 巻 33, p. 60-85, 発行日 2004-03 |
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| 出版者 | ||||||
| 出版者 | 京都産業大学 | |||||
| ISSN | ||||||
| 収録物識別子タイプ | PISSN | |||||
| 収録物識別子 | 1348-3323 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA11923897 | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
