L-Glutamate Secretion by the N-Terminal Domain of the Corynebacterium glutamicum NCgl1221 Mechanosensitive Channel
-
- YAMASHITA Chikako
- Department of Bioengineering, Tokyo Institute of Technology
-
- HASHIMOTO Ken-ichi
- Department of Green and Sustainable Chemistry, Tokyo Denki University
-
- KUMAGAI Kosuke
- Department of Bioengineering, Tokyo Institute of Technology
-
- MAEDA Tomoya
- Department of Bioengineering, Tokyo Institute of Technology
-
- TAKADA Ayako
- Technical Department, Tokyo Institute of Technology
-
- YABE Isamu
- Department of Green and Sustainable Chemistry, Tokyo Denki University
-
- KAWASAKI Hisashi
- Department of Green and Sustainable Chemistry, Tokyo Denki University
-
- WACHI Masaaki
- Department of Bioengineering, Tokyo Institute of Technology
書誌事項
- タイトル別名
-
- <small>L</small>-Glutamate Secretion by the N-Terminal Domain of the <i>Corynebacterium glutamicum</i> NCgl1221 Mechanosensitive Channel
- <scp>L</scp>-Glutamate Secretion by the N-Terminal Domain of the<i>Corynebacterium glutamicum</i>NCgl1221 Mechanosensitive Channel
この論文をさがす
抄録
The Corynebacterium glutamicum NCgl1221 mechanosensitive channel mediates L-glutamate secretion by sensing changes in membrane tension caused by treatments such as biotin limitation and penicillin. The NCgl1221 protein has an N-terminal domain (1–286 a.a.) homologous to the Escherichia coli MscS and a long C-terminal domain (287–533 a.a.) of unknown function. In order to investigate the role of the C-terminal domain in L-glutamate secretion, we constructed a series of C-terminally truncated mutants of NCgl1221. We found that the N-terminal domain, homologous to E. coli MscS, retained the ability to cause L-glutamate secretion in response to the treatment. Electrophysiological analysis confirmed that the N-terminal domain mediated L-glutamate secretion. 3D homology modeling has suggested that the N-terminal domain of NCgl1221 has an extra loop structure (221–232 a.a.) that is not found in most other MscS proteins. The mutant NCgl1221, deleted for this loop structure, lost the ability to secrete L-glutamate. In addition, we found that mutant NCgl1221 lacking the C-terminal extracytoplasmic domain (420–533 a.a.) produced L-glutamate without any inducing treatment. These results suggest that the N-terminal domain is necessary and sufficient for the excretion of L-glutamate in response to inducing treatment, and that the C-terminal extracytoplasmic domain has a negative regulatory role in L-glutamate production.
収録刊行物
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 77 (5), 1008-1013, 2013
公益社団法人 日本農芸化学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390001206478002944
-
- NII論文ID
- 10031177589
-
- NII書誌ID
- AA10824164
-
- COI
- 1:STN:280:DC%2BC3snht1ChsA%3D%3D
-
- ISSN
- 13476947
- 09168451
-
- NDL書誌ID
- 024526084
-
- PubMed
- 23649271
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
-
- 抄録ライセンスフラグ
- 使用不可