三量体オートトランスポーターの構造形成機構に関する研究

Persistent ID (NDL): info:ndljp/pid/13023815

Material type: 博士論文

Author: 青木, 英莉子ほか

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Publication date: 2018-03-18

Material Format: Digital

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Name of awarding university/degree: 創価大学,博士（工学）

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Note (General)：: Haemophilus influenzae adhesin (Hia) belongs to the trimeric autotransporter family and consists of a passengerdomain and a transmembrane domain (HiaT...

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Material Type: 博士論文
Title: 三量体オートトランスポーターの構造形成機構に関する研究
Author/Editor: 青木, 英莉子
AOKI, Eriko
Author Heading: 青木, 英莉子
AOKI, Eriko
Publication Date: 2018-03-18
Publication Date (W3CDTF): 2018-03-18
Alternative Title: A study on the folding and assembly mechanism of a trimeric autotransporter
Degree grantor/type: 創価大学
Date Granted: 2018-03-18
Date Granted (W3CDTF): 2018-03-18
Dissertation Number: 甲第158号
Degree Type: 博士（工学）
Text Language Code: jpn
Subject Heading: trimeric autotransporter
bacteria secretion system
reassembly kinetics
arginine cluster
Target Audience: 一般
Note (General): Haemophilus influenzae adhesin (Hia) belongs to the trimeric autotransporter family and consists of a passengerdomain and a transmembrane domain (HiaT). HiaT forms a 12-stranded transmembrane b-barrel. This protein has aunique arginine residue at 1077. Arg1077 side chains from three subunits protrude toward the center of the barreland close to each other. The arrangement seems to be unfavorable for trimer assembly because of repulsionbetween the positive charges. To investigate the role of this residue on trimer assembly, we prepared two mutants,R1077M and R1077K, in which arginine at 1077 was replaced with methionine and lysine, respectively. The proteinswere expressed using an expression system developed in this study and purified for assembly experiments. Assemblyexperiments indicate that the neutralization of R1077 positive charge accelerated the rate of assembly butdecreased the amount of the correctly assembled trimer. The result suggests that the repulsion between uniquearginine residues is important for preventing HiaT from misassembly.
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Date Accepted (W3CDTF): 2023-10-11T15:41:04+09:00
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Periodical Title (URI): http://hdl.handle.net/10911/00039387
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