NDLI: Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5.

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Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5.

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Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schuler, M. A. Jollie, D. R. Beck Von Bodman, S. Sligar, S. G.
Abstract	We have totally synthesized a gene that codes for rat hepatic cytochrome b5. The 5' flanking region was designed for efficient expression of this gene in Escherichia coli by incorporating an optimum ribosome binding site and spacer region. Both a soluble form, analogous to the protease-treated microsomal protein, as well as the complete cytochrome with hydrophobic membrane anchor, was constructed and expressed. Transformants with the gene for the soluble protein overproduce authentic cytochrome b5 to a level of 8% of the total cell protein. The complete cytochrome is expressed to a lesser extent with most of the protein found in the cell membrane fraction. This represents complete synthesis and bacterial expression of a mammalian metalloprotein gene. Cytochrome b5 is normally a six-coordinate low spin heme protein with histidine-39 and histidine-63 as axial ligands. We have replaced histidine-63 with a methionine residue by cassette mutagenesis, utilizing specific restriction enzyme sites engineered into the synthetic gene. The resultant protein has histidine-39 as sole axial ligand and is five-coordinate high spin in the ferric resting state, as indicated by optical and electron spin resonance spectroscopy. The ability to generate mutant cytochrome b5 in high yield is a crucial step in understanding heme protein folding, protein-protein recognition and binding, and biological electron transfer processes.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome b Group Genetics Animals Cloning, Molecular Cytochromes B5 DNA Chemical Synthesis Escherichia Coli Genes Genetic Engineering Membrane Proteins Microsomes, Liver Enzymology Mutation Spectrum Analysis Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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