Cotranslational folding of human growth hormone in vitro and in Escherichia coli

被引：1

作者：

Mermans, Daphne ^{[1
,4
]}

Nicolaus, Felix ^{[1
]}

Baygin, Aysel ^{[1
]}

von Heijne, Gunnar ^{[1
,2
,3
]}

机构：

[1] Stockholm Univ, Dept Biochem & Biophys, Stockholm, Sweden

[2] Stockholm Univ, Sci Life Lab, Solna, Sweden

[3] Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden

[4] Fontys Univ Appl Sci, Eindhoven, Netherlands

来源：

FEBS LETTERS | 2023年 / 597卷 / 10期

基金：

瑞典研究理事会;

关键词：

cotranslational protein folding; human growth hormone; NASCENT-CHAIN; ARREST; EXPRESSION; SECM;

D O I：

10.1002/1873-3468.14562

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human growth hormone (hGH) is a four-helix bundle protein of considerable pharmacological interest. Recombinant hGH is produced in bacteria, yet little is known about its folding during expression in Escherichia coli. We have studied the cotranslational folding of hGH using force profile analysis (FPA), both during in vitro translation in the absence and presence of the chaperone trigger factor (TF), and when expressed in E. coli. We find that the main folding transition starts before hGH is completely released from the ribosome, and that it can interact with TF and possibly other chaperones.

引用

页码：1355 / 1362

页数：8

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