Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

Clemens Vonrhein; Ulrich Schmidt; Gabriele A. Ziegler; Susann Schweiger; Israel Hanukoglu; Georg E. Schulz

doi:10.1016/S0014-5793(98)01714-1

Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

Clemens Vonrhein
, Ulrich Schmidt
, Gabriele A. Ziegler
, Susann Schweiger
, Israel Hanukoglu
, Georg E. Schulz

Department of Molecular Biology

نتاج البحث: نشر في مجلة › مقالة › مراجعة النظراء

24 اقتباسات (Scopus)

ملخص

Adrenodoxin reductase is an essential component of the mitochondrial monooxygenase systems that are involved in the synthesis of steroid hormones and related compounds. After removing by mutagenesis a secondary ribosome binding site and an mRNA loop formed between the gene and the vector, large amounts of the enzyme could be produced in Escherichia coli by coexpression with the HSP60-chaperone system. The purified protein was homogeneous enough for reproducible crystallization. The crystals diffracted X-rays isotropically beyond 1.7 A resolution permitting a structure analysis. Copyright (C) 1999 Federation of European Biochemical Societies.

اللغة الأصلية	الإنجليزيّة
الصفحات (من إلى)	167-169
عدد الصفحات	3
دورية	FEBS Letters
مستوى الصوت	443
رقم الإصدار	2
المعرِّفات الرقمية للأشياء	https://doi.org/10.1016/S0014-5793(98)01714-1
حالة النشر	نُشِر - 29 يناير 1999

الوصول إلى المستند

10.1016/S0014-5793(98)01714-1

الملفات والروابط الأخرى

Link to publication in Scopus

قم بذكر هذا

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title = "Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli",

abstract = "Adrenodoxin reductase is an essential component of the mitochondrial monooxygenase systems that are involved in the synthesis of steroid hormones and related compounds. After removing by mutagenesis a secondary ribosome binding site and an mRNA loop formed between the gene and the vector, large amounts of the enzyme could be produced in Escherichia coli by coexpression with the HSP60-chaperone system. The purified protein was homogeneous enough for reproducible crystallization. The crystals diffracted X-rays isotropically beyond 1.7 A resolution permitting a structure analysis. Copyright (C) 1999 Federation of European Biochemical Societies.",

keywords = "Adrenodoxin reductase, Chaperone coexpression, Crystallization, Secondary ribosome binding site, mRNA loop",

author = "Clemens Vonrhein and Ulrich Schmidt and Ziegler, \{Gabriele A.\} and Susann Schweiger and Israel Hanukoglu and Schulz, \{Georg E.\}",

note = "Funding Information: We thank Dr. G. Brenner and Dr. D. Hochman (Marbek Ltd., Kiriat Malachi, Israel) for the bovine adrenals, Dr. Y. Sagara (Kochi Medical School, Japan) for plasmid pBAR1607 encoding bovine adrenodoxin reductase, P. Caspers (Hoffmann-La Roche, Basel, Switzerland) for the plasmids pREP4-groESL and pRDKJG, G. Steglich for help in cloning experiments, and the EMBL outstation team in Hamburg for help in data collection. The work was supported by the Deutsche Forschungsgemeinschaft under Sfb-388. ",

year = "1999",

month = jan,

day = "29",

doi = "10.1016/S0014-5793(98)01714-1",

language = "אנגלית",

volume = "443",

pages = "167--169",

journal = "FEBS Letters",

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TY - JOUR

T1 - Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

AU - Vonrhein, Clemens

AU - Schmidt, Ulrich

AU - Ziegler, Gabriele A.

AU - Schweiger, Susann

AU - Hanukoglu, Israel

AU - Schulz, Georg E.

N1 - Funding Information: We thank Dr. G. Brenner and Dr. D. Hochman (Marbek Ltd., Kiriat Malachi, Israel) for the bovine adrenals, Dr. Y. Sagara (Kochi Medical School, Japan) for plasmid pBAR1607 encoding bovine adrenodoxin reductase, P. Caspers (Hoffmann-La Roche, Basel, Switzerland) for the plasmids pREP4-groESL and pRDKJG, G. Steglich for help in cloning experiments, and the EMBL outstation team in Hamburg for help in data collection. The work was supported by the Deutsche Forschungsgemeinschaft under Sfb-388.

PY - 1999/1/29

Y1 - 1999/1/29

N2 - Adrenodoxin reductase is an essential component of the mitochondrial monooxygenase systems that are involved in the synthesis of steroid hormones and related compounds. After removing by mutagenesis a secondary ribosome binding site and an mRNA loop formed between the gene and the vector, large amounts of the enzyme could be produced in Escherichia coli by coexpression with the HSP60-chaperone system. The purified protein was homogeneous enough for reproducible crystallization. The crystals diffracted X-rays isotropically beyond 1.7 A resolution permitting a structure analysis. Copyright (C) 1999 Federation of European Biochemical Societies.

AB - Adrenodoxin reductase is an essential component of the mitochondrial monooxygenase systems that are involved in the synthesis of steroid hormones and related compounds. After removing by mutagenesis a secondary ribosome binding site and an mRNA loop formed between the gene and the vector, large amounts of the enzyme could be produced in Escherichia coli by coexpression with the HSP60-chaperone system. The purified protein was homogeneous enough for reproducible crystallization. The crystals diffracted X-rays isotropically beyond 1.7 A resolution permitting a structure analysis. Copyright (C) 1999 Federation of European Biochemical Societies.

KW - Adrenodoxin reductase

KW - Chaperone coexpression

KW - Crystallization

KW - Secondary ribosome binding site

KW - mRNA loop

UR - https://www.scopus.com/pages/publications/0033065348

U2 - 10.1016/S0014-5793(98)01714-1

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C2 - 9989598

AN - SCOPUS:0033065348

SN - 0014-5793

VL - 443

SP - 167

EP - 169

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

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