Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium

Jae Hwan Lim; Yeon Gyu Yu; In Geol Choi; Jae Ryeon Ryu; Byung Yoon Ahn; Sung Hou Kim; Ye Sun Han

doi:10.1016/S0014-5793(97)00262-7

Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium

Jae Hwan Lim, Yeon Gyu Yu, In Geol Choi, Jae Ryeon Ryu, Byung Yoon Ahn, Sung Hou Kim, Ye Sun Han

Department of Life Sciences

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

35 Citations (Scopus)

Abstract

A superoxide dismutase (SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homooligomeric protein with a monomeric molecular mass of 24.2 kDa. The DNA-derived amino acid sequence is more similar to those of known Mn- and Fe-SODs from thermophilic archaea than of Cu, Zn-SODs. The metal binding residues found in all SOD sequences from different species are also conserved in A. pyrophilus SOD. The protein is biochemically active only as an oligomer and is resistant to thermal denaturation.

Original language	English
Pages (from-to)	142-146
Number of pages	5
Journal	FEBS Letters
Volume	406
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(97)00262-7
Publication status	Published - 1997 Apr 7

Keywords

Aquifex
Hyperthermophile
Superoxide dismutase
Thermostability

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/S0014-5793(97)00262-7

Cite this

@article{1939834ce9354d9a952c963b8abe790d,

title = "Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium",

abstract = "A superoxide dismutase (SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homooligomeric protein with a monomeric molecular mass of 24.2 kDa. The DNA-derived amino acid sequence is more similar to those of known Mn- and Fe-SODs from thermophilic archaea than of Cu, Zn-SODs. The metal binding residues found in all SOD sequences from different species are also conserved in A. pyrophilus SOD. The protein is biochemically active only as an oligomer and is resistant to thermal denaturation.",

keywords = "Aquifex, Hyperthermophile, Superoxide dismutase, Thermostability",

author = "Lim, {Jae Hwan} and Yu, {Yeon Gyu} and Choi, {In Geol} and Ryu, {Jae Ryeon} and Ahn, {Byung Yoon} and Kim, {Sung Hou} and Han, {Ye Sun}",

note = "Funding Information: We thank Dr. Rosalind Kim for her advise and participation in the preparation of the manuscript. We gratefully acknowledge the support of Korea Institute of Science and Technology and a grant from Ministry of Science and Technology, Korea. The work of S.-H. Kim was supported by US Department of Energy (DOE-AC03-76S00098).",

year = "1997",

month = apr,

day = "7",

doi = "10.1016/S0014-5793(97)00262-7",

language = "English",

volume = "406",

pages = "142--146",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium

AU - Lim, Jae Hwan

AU - Yu, Yeon Gyu

AU - Choi, In Geol

AU - Ryu, Jae Ryeon

AU - Ahn, Byung Yoon

AU - Kim, Sung Hou

AU - Han, Ye Sun

N1 - Funding Information: We thank Dr. Rosalind Kim for her advise and participation in the preparation of the manuscript. We gratefully acknowledge the support of Korea Institute of Science and Technology and a grant from Ministry of Science and Technology, Korea. The work of S.-H. Kim was supported by US Department of Energy (DOE-AC03-76S00098).

PY - 1997/4/7

Y1 - 1997/4/7

N2 - A superoxide dismutase (SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homooligomeric protein with a monomeric molecular mass of 24.2 kDa. The DNA-derived amino acid sequence is more similar to those of known Mn- and Fe-SODs from thermophilic archaea than of Cu, Zn-SODs. The metal binding residues found in all SOD sequences from different species are also conserved in A. pyrophilus SOD. The protein is biochemically active only as an oligomer and is resistant to thermal denaturation.

AB - A superoxide dismutase (SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homooligomeric protein with a monomeric molecular mass of 24.2 kDa. The DNA-derived amino acid sequence is more similar to those of known Mn- and Fe-SODs from thermophilic archaea than of Cu, Zn-SODs. The metal binding residues found in all SOD sequences from different species are also conserved in A. pyrophilus SOD. The protein is biochemically active only as an oligomer and is resistant to thermal denaturation.

KW - Aquifex

KW - Hyperthermophile

KW - Superoxide dismutase

KW - Thermostability

UR - http://www.scopus.com/inward/record.url?scp=0030914069&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(97)00262-7

DO - 10.1016/S0014-5793(97)00262-7

M3 - Article

C2 - 9109405

AN - SCOPUS:0030914069

SN - 0014-5793

VL - 406

SP - 142

EP - 146

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this