YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3)

Keum Young Ahn; Jin Seung Park; Kyung Yeon Han; Jong Am Song; Jeewon Lee

doi:10.1016/j.febslet.2012.02.051

YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3)

Keum Young Ahn, Jin Seung Park, Kyung Yeon Han, Jong Am Song, Jeewon Lee

Department of Chemical and Biological Engineering

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

Escherichia coli YrhB (10.6 kDa) from strain BL21(DE3) that is commonly used for protein overexpression is a stable chaperone-like protein and indispensable for supporting the growth of BL21(DE3) at 48 °C but not defined as conventional heat shock protein (HSP). YrhB effectively prevented heat-induced aggregation of ribonucleotide synthetase (PurK). Without ATP, YrhB alone promoted in vitro refolding of uridine phosphorylase (UDP) and protected thermal denaturation of the refolded UDP. As a cis-acting fusion partner, YrhB also significantly reduced inclusion body formation of nine aggregation-prone heterologous proteins in BL21(DE3). Unlike conventional small HSPs, YrhB remained monomer under heat shock condition.

Original language	English
Pages (from-to)	1044-1048
Number of pages	5
Journal	FEBS Letters
Volume	586
Issue number	7
DOIs	https://doi.org/10.1016/j.febslet.2012.02.051
Publication status	Published - 2012 Apr 5

Keywords

BL21(DE3)
Chaperone-like protein
Heat shock
YrhB

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2012.02.051

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title = "YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3)",

abstract = "Escherichia coli YrhB (10.6 kDa) from strain BL21(DE3) that is commonly used for protein overexpression is a stable chaperone-like protein and indispensable for supporting the growth of BL21(DE3) at 48 °C but not defined as conventional heat shock protein (HSP). YrhB effectively prevented heat-induced aggregation of ribonucleotide synthetase (PurK). Without ATP, YrhB alone promoted in vitro refolding of uridine phosphorylase (UDP) and protected thermal denaturation of the refolded UDP. As a cis-acting fusion partner, YrhB also significantly reduced inclusion body formation of nine aggregation-prone heterologous proteins in BL21(DE3). Unlike conventional small HSPs, YrhB remained monomer under heat shock condition.",

keywords = "BL21(DE3), Chaperone-like protein, Heat shock, YrhB",

author = "Ahn, {Keum Young} and Park, {Jin Seung} and Han, {Kyung Yeon} and Song, {Jong Am} and Jeewon Lee",

note = "Funding Information: This study was supported by the National Research Laboratory Project (grant no. 2011-0020464 , the main project that supported this work), the Microbial Genomics and Applications Center at KRIBB (grant no. 2011-K000406 ), the Public Welfare & Safety research program (grant no. 2011-0021116 ), and the Basic Science Research Program (ERC program, grant no. 2011-0000874 ) of the National Research Foundation of Korea (NRF) grant funded by the Korea government. This work was also supported by Korea University and National Research Foundation of Korea (NRF) (grant no. 2011-0027538 ). ",

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doi = "10.1016/j.febslet.2012.02.051",

language = "English",

volume = "586",

pages = "1044--1048",

journal = "FEBS Letters",

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AU - Ahn, Keum Young

AU - Park, Jin Seung

AU - Han, Kyung Yeon

AU - Song, Jong Am

AU - Lee, Jeewon

N1 - Funding Information: This study was supported by the National Research Laboratory Project (grant no. 2011-0020464 , the main project that supported this work), the Microbial Genomics and Applications Center at KRIBB (grant no. 2011-K000406 ), the Public Welfare & Safety research program (grant no. 2011-0021116 ), and the Basic Science Research Program (ERC program, grant no. 2011-0000874 ) of the National Research Foundation of Korea (NRF) grant funded by the Korea government. This work was also supported by Korea University and National Research Foundation of Korea (NRF) (grant no. 2011-0027538 ).

PY - 2012/4/5

Y1 - 2012/4/5

N2 - Escherichia coli YrhB (10.6 kDa) from strain BL21(DE3) that is commonly used for protein overexpression is a stable chaperone-like protein and indispensable for supporting the growth of BL21(DE3) at 48 °C but not defined as conventional heat shock protein (HSP). YrhB effectively prevented heat-induced aggregation of ribonucleotide synthetase (PurK). Without ATP, YrhB alone promoted in vitro refolding of uridine phosphorylase (UDP) and protected thermal denaturation of the refolded UDP. As a cis-acting fusion partner, YrhB also significantly reduced inclusion body formation of nine aggregation-prone heterologous proteins in BL21(DE3). Unlike conventional small HSPs, YrhB remained monomer under heat shock condition.

AB - Escherichia coli YrhB (10.6 kDa) from strain BL21(DE3) that is commonly used for protein overexpression is a stable chaperone-like protein and indispensable for supporting the growth of BL21(DE3) at 48 °C but not defined as conventional heat shock protein (HSP). YrhB effectively prevented heat-induced aggregation of ribonucleotide synthetase (PurK). Without ATP, YrhB alone promoted in vitro refolding of uridine phosphorylase (UDP) and protected thermal denaturation of the refolded UDP. As a cis-acting fusion partner, YrhB also significantly reduced inclusion body formation of nine aggregation-prone heterologous proteins in BL21(DE3). Unlike conventional small HSPs, YrhB remained monomer under heat shock condition.

KW - BL21(DE3)

KW - Chaperone-like protein

KW - Heat shock

KW - YrhB

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ER -

YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3)

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Keywords

ASJC Scopus subject areas

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