The effects of L-arginine on protein stability and DNA binding ability of SaeR, a transcription factor in Staphylococcus aureus

被引：6

作者：

Fan, Ruochen ^{[1
,2
]}

Shi, Xian ^{[2
]}

Guo, Binmei ^{[2
]}

Zhao, Jing ^{[2
]}

Liu, Jialu ^{[2
]}

Quan, Chunshan ^{[2
]}

Dong, Yuesheng ^{[1
]}

Fan, Shengdi ^{[2
]}

机构：

[1] Dalian Univ Technol, Sch Bioengn, Dalian, Peoples R China

[2] Dalian Minzu Univ, Coll Life Sci, Key Lab Biotechnol & Bioresources Utilizat, Minist Educ, Dalian, Peoples R China

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2021年 / 177卷

基金：

中国国家自然科学基金;

关键词：

SaeRS two-component system; SaeR; L-arginine; Staphylococcus aureus; RESPONSE REGULATOR SAER; 2-COMPONENT SYSTEM; VIRULENCE FACTORS; AMINO-ACIDS; PROMOTER;

D O I：

10.1016/j.pep.2020.105765

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The SaeRS two-component system in Staphylococcus aureus controls the expression of a series of virulence factors, such as hemolysins, pmteases, and coagulase. The response regulator, SaeR, belongs to the OmpR family with an N-terminal regulatory domain and a C-terminal DNA binding domain. To improve the production and stability of the recombinant protein SaeR, L-arginine (L-Arg) was added to the purification buffers. L-Arg enhanced the solubility and stability of the recombinant protein SaeR. The thermal denaturation temperature of SaeR in 10 mM L-Arg buffer was significantly increased compared to the buffer without L-Arg. Microscale Thermophoresis (MST) analysis results showed that the SaeR protein could bind to the P1 promoter under both phosphorylated and non-phosphorylated status in buffer containing 10 mM L-Arg. These results illustrate an effective method to purify SaeR and other proteins.

引用

页数：7