Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli

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

doi:10.1007/s10529-007-9417-3

Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli

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

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

8 Citations (Scopus)

Abstract

Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.

Original language	English
Pages (from-to)	1513-1518
Number of pages	6
Journal	Biotechnology letters
Volume	29
Issue number	10
DOIs	https://doi.org/10.1007/s10529-007-9417-3
Publication status	Published - 2007 Oct

Bibliographical note

Funding Information:
Acknowledgements We thank Professor Hang Chul Shin at Soongsil University for kindly providing the gene clones of mpINS and G-CSF. We also appreciate Professors Won Tae Lee and Hyun Soo Cho at Yonsei University for the kind donation of ppGRN, AID, and Nacht clones, respectively. This study was supported by the Korea Health 21 R&D Project of the Ministry of Health & Welfare of the Republic of Korea (grant no. A050750). This work was also supported by the Second Brain Korea 21 Project. Further supports from the Korea Science and Engineering Foundation (grant no. R01-2005-000-10355-0), the Korea Research Foundation (grant no. KRF-2004-041-D00180), and the Microbial Genomics & Applications Center (Taejon, Republic of Korea) are also appreciated.

Keywords

Escherichia coli proteome
Malate dehydrogenase
Solubility enhancer
Stress response

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-007-9417-3

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title = "Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli",

abstract = "Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.",

keywords = "Escherichia coli proteome, Malate dehydrogenase, Solubility enhancer, Stress response",

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note = "Funding Information: Acknowledgements We thank Professor Hang Chul Shin at Soongsil University for kindly providing the gene clones of mpINS and G-CSF. We also appreciate Professors Won Tae Lee and Hyun Soo Cho at Yonsei University for the kind donation of ppGRN, AID, and Nacht clones, respectively. This study was supported by the Korea Health 21 R&D Project of the Ministry of Health & Welfare of the Republic of Korea (grant no. A050750). This work was also supported by the Second Brain Korea 21 Project. Further supports from the Korea Science and Engineering Foundation (grant no. R01-2005-000-10355-0), the Korea Research Foundation (grant no. KRF-2004-041-D00180), and the Microbial Genomics & Applications Center (Taejon, Republic of Korea) are also appreciated.",

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AU - Song, Jong Am

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AU - Seo, Hyuk Seong

AU - Lee, Jeewon

N1 - Funding Information: Acknowledgements We thank Professor Hang Chul Shin at Soongsil University for kindly providing the gene clones of mpINS and G-CSF. We also appreciate Professors Won Tae Lee and Hyun Soo Cho at Yonsei University for the kind donation of ppGRN, AID, and Nacht clones, respectively. This study was supported by the Korea Health 21 R&D Project of the Ministry of Health & Welfare of the Republic of Korea (grant no. A050750). This work was also supported by the Second Brain Korea 21 Project. Further supports from the Korea Science and Engineering Foundation (grant no. R01-2005-000-10355-0), the Korea Research Foundation (grant no. KRF-2004-041-D00180), and the Microbial Genomics & Applications Center (Taejon, Republic of Korea) are also appreciated.

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N2 - Using 2-dimensional gel electrophoresis, the Escherichia coli proteome response to a heat-shock stress was analyzed and a 1.6-fold increase of malate dehydrogenase was observed even under the heat-shock condition where the total number of soluble proteins decreased by about 5%. We subsequently demonstrated that, as an N-terminus fusion expression partner, malate dehydrogenase facilitated the folding of, and dramatically increased the solubility of, many aggregation-prone heterologous proteins in E. coli cytoplasm. Therefore, malate dehydrogenase is well suited for production of a biologically active fusion mutant of cutinase (Pseudomonas putida origin) that is currently of considerable to biotechnology and commercial industries.

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Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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