Abstract
The genes coding for plastocyanin (petE) and cytochrome c6 (petJ) from Anabaena sp. PCC 7119 have been cloned and properly expressed in Escherichia coli. The recombinant proteins are identical to those purified from the cyanobacterial cells. The products of both the petE and petJ genes are correctly processed in E. coli, as deduced from their identical N-terminal amino acid sequences as compared with those of the metalloproteins isolated from the cyanobacterium. Physicochemical and functional properties of the native and recombinant protein preparations are also identical, thereby confirming that expression of petE and petJ genes in E. coli is an adequate tool to address the study of the structure/function relationships in plastocyanin and cytochrome c6 from Anabaena by site-directed mutagenesis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anabaena / genetics*
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Base Sequence
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Cloning, Molecular
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Cytochrome c Group / chemistry
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Cytochrome c Group / genetics*
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Cytochrome c Group / metabolism
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Cytochromes / chemistry
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Cytochromes / genetics*
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Cytochromes / metabolism
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Cytochromes f
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DNA / genetics
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DNA Primers / genetics
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Gene Expression
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Genes, Bacterial*
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Molecular Sequence Data
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Plastocyanin / chemistry
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Plastocyanin / genetics*
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Plastocyanin / metabolism
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Protein Processing, Post-Translational
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Spectrophotometry
Substances
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Cytochrome c Group
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Cytochromes
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DNA Primers
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Recombinant Proteins
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cytochrome c553
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DNA
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Plastocyanin
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Cytochromes f
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cytochrome C-552
Associated data
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GENBANK/AJ002361
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GENBANK/AJ002362