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Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis.
http://hdl.handle.net/10069/22179
http://hdl.handle.net/10069/2217949ef6d0f-f4f7-4738-9b30-bb785fbf885a
名前 / ファイル | ライセンス | アクション |
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BioChe389_1209.pdf (449.4 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2009-09-17 | |||||
タイトル | ||||||
タイトル | Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis. | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | prepro-segment | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | recombinant protein | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | signal sequence | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Staphylococcus epidermidis | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | thermolysin | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | V8 protease | |||||
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 | journal article | |||||
著者 |
Ohara-Nemoto, Yuko
× Ohara-Nemoto, Yuko× Ono, Toshio× Shimoyama, Yu× Kimura, Shigenobu× Nemoto, Takayuki K |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The extracellular serine endopeptidase GluSE (EC 3.4.21.19) is considered to be one of the virulence factors of Staphylococcus epidermidis. The present study investigated maturation processing of native GluSE and that heterologously expressed in Escherichia coli. In addition to the 28-kDa mature protease, small amounts of proenzymes with molecular masses of 32, 30, and 29 kDa were identified in the extracellular and cell wall-associated fractions. We defined the pre (M1-A27)- and pro (K28-S66)-segments, and found that processing at the E32-S33 and D48-I49 bonds was responsible for production of the 30- and 29-kDa intermediates, respectively. The full-length form of C-terminally His-tagged GluSE was purified as three proenzymes equivalent to the native ones. These molecules possessing an entire or a part of the pro-segment were proteolytically latent and converted to a mature 28-kDa form by thermolysin cleavage at the S66-V67 bond. Mutation of the essential amino acid S235 suggested auto-proteolytic production of the 30- and 29-kDa intermediates. Furthermore, an undecapeptide (I56-S66) of the truncated pro-segment not only functions as an inhibitor of the protease but also facilitates thermolysin processing. These findings could offer clues to the molecular mechanism involved in the regulation of proteolytic activity of pathogenic proteases secreted from S. epidermidis. | |||||
書誌情報 |
Biological chemistry, 389(9), 1209-1217; 2008 巻 389, 号 9, p. 1209-1217, 発行日 2008-09 |
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出版者 | ||||||
出版者 | Walter de Gruyter | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 14316730 | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1437-4315 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 18783343 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1515/BC.2008.137 | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Biological Chemistry, 389(9), pp.1209-1217; 2008 |