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  1. 080 繊維学部
  2. 0801 学術論文

Synthetic Lethality of the lytE cwlO Genotype in Bacillus subtilis Is Caused by Lack of D,L-Endopeptidase Activity at the Lateral Cell Wall

http://hdl.handle.net/10091/16187
http://hdl.handle.net/10091/16187
e27a880d-96a1-4343-8a11-8d69f6698ff1
名前 / ファイル ライセンス アクション
synthetic_lethality_lytE_cwlO_Bacillus.pdf synthetic_lethality_lytE_cwlO_Bacillus.pdf (2.7 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-01-18
タイトル
言語 en
タイトル Synthetic Lethality of the lytE cwlO Genotype in Bacillus subtilis Is Caused by Lack of D,L-Endopeptidase Activity at the Lateral Cell Wall
言語
言語 eng
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
著者 Hashimoto, Masayuki

× Hashimoto, Masayuki

WEKO 40649

Hashimoto, Masayuki

Search repository
Ooiwa, Seika

× Ooiwa, Seika

WEKO 40650

Ooiwa, Seika

Search repository
Sekiguchi, Junichi

× Sekiguchi, Junichi

WEKO 40651

Sekiguchi, Junichi

Search repository
出版者
出版者 AMER SOC MICROBIOLOGY
引用
内容記述タイプ Other
内容記述 JOURNAL OF BACTERIOLOGY. 194(4):796-803 (2012)
書誌情報 JOURNAL OF BACTERIOLOGY

巻 194, 号 4, p. 796-803, 発行日 2012-02
抄録
内容記述タイプ Abstract
内容記述 Bacterial peptidoglycan acts as an exoskeleton to protect the bacterial cell. Although peptidoglycan biosynthesis by penicillin-binding proteins is well studied, few studies have described peptidoglycan disassembly, which is necessary for a dynamic structure that allows cell growth. In Bacillus subtilis, more than 35 genes encoding cell wall lytic enzymes have been identified; however, only two D,L-endopeptidases (lytE and cwlO) are involved in cell proliferation. In this study, we demonstrated that the D,L-endopeptidase activity at the lateral cell wall is essential for cell proliferation. Inactivation of LytE and CwlO by point mutation of the catalytic residues caused cell growth defects. However, the forced expression of LytF or CwlS, which are paralogs of LytE, did not suppress lytE cwlO synthetic lethality. Subcellular localization studies of these D,L-endopeptidases showed LytE and CwlS at the septa and poles, CwlO at the cylindrical part of the cell, and LytE at the septa and poles as well as the cylindrical part. Furthermore, construction of N-terminal and C-terminal domain-swapped enzymes of LytE, LytF, CwlS, and CwlO revealed that localization was dependent on the N-terminal domains. Only the chimeric proteins that were enzymatically active and localized to the sidewall were able to suppress the synthetic lethality, suggesting that the lack of D,L-endopeptidase activity at the cylindrical part of the cell leads to a growth defect. The functions of LytE and CwlO in cell morphogenesis were discussed.
資源タイプ(コンテンツの種類)
内容記述タイプ Other
内容記述 Article
ISSN
収録物識別子タイプ ISSN
収録物識別子 0021-9193
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA0069403X
PubMed
識別子タイプ PMID
関連識別子 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=22139507
関連名称 22139507
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1128/JB.05569-11
関連名称 10.1128/JB.05569-11
権利
権利情報 Copyright© 2012 American Society for Microbiology.
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
WoS
表示名 Web of Science
URL http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000299966000006
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