Functional characterization of an additional transmembrane domain unique to TrkG and TrkH in Escherichia coli.

IF 1.3 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Bioscience, Biotechnology, and Biochemistry Pub Date : 2025-09-23 DOI:10.1093/bbb/zbaf101

Ellen Tanudjaja, Haoyu Zhang, Tadaomi Furuta, Masaru Tsujii, Yasuhiro Ishimaru, Nobuyuki Uozumi

引用次数: 0

Abstract

Escherichia coli TrkG and TrkH transporters contain a unique N-terminal Domain-0 (D0). Our findings reveal that D0 supports both the function and stability of TrkG, enabling K+ and Na+ uptake, whereas it is not essential for TrkH-mediated K+ uptake. This difference can be attributed to D0 role in stabilizing polar residues within TrkG core transmembrane domains.

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大肠杆菌中TrkG和TrkH独有的额外跨膜结构域的功能表征。

大肠杆菌TrkG和TrkH转运体含有一个独特的n端Domain-0 （D0）。我们的研究结果表明，D0支持TrkG的功能和稳定性，使K+和Na+摄取，而不是trkh介导的K+摄取所必需的。这种差异可归因于D0在TrkG核心跨膜结构域中稳定极性残基的作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Bioscience, Biotechnology, and Biochemistry 生物-生化与分子生物学

CiteScore

3.50

自引率

0.00%

发文量

183

审稿时长

1 months

期刊介绍： Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).