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  Expression in Escherichia coli of c-type cytochrome genes from Rhodopseudomonas viridis

Grisshammer, R., Oeckl, C., & Michel, H. (1991). Expression in Escherichia coli of c-type cytochrome genes from Rhodopseudomonas viridis. Biochimica et Biophysica Acta-Gene Structure and Expression, 1088(2), 183-190. doi:10.1016/0167-4781(91)90053-O.

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 Creators:
Grisshammer, Reinhard1, Author              
Oeckl, Christine1, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Cytochrome; c-type; Gene expression; Inclusion body; (Escherichia coli); (Rhodopseudomonas viridis)
 Abstract: The genes coding for the photosynthetic reaction center cytochrome c subunit (pufC) and the soluble cytochrome c2 (cycA) from the purple non-sulfur bacterium Rhodopseudomonas viridis were expressed in Escherichia coli. Biosynthesis of the reaction center cytochrome without a signal peptide resulted in the formation of inclusion bodies in the cytoplasm amounting to 14% of the total cellular protein. A series of plasmids coding for the cytochrome subunit with varying N-terminal signal peptides was constructed in attempts to achieve translocation across the E. coli cytoplasmic membrane and heme attachment. However, the two major recombinant proteins with N-termini corresponding to the signal peptide and the cytochrome were synthesized in E. coli as non-specific aggregates without heme incorporation. An increased ratio of precursor as compared to ‘processed’ apo-cytochrome was obtained when expression was carried out in a proteinase-deficient strain. Cytochrome c2 from R. viridis was synthesized in E. coli as a precursor associated with the cytoplasmic membrane. An expression plasmid was designed encoding the N-terminal part of the 33 kDa precursor protein of the oxygen-evolving complex of Photosystem II from spinach followed by cytochrome c2. Two recombinant proteins without heme were found to aggregate as inclusion bodies with N-termini corresponding to the signal peptide and the mature 33 kDa protein.

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Language(s): eng - English
 Dates: 1990-06-161003-03-241991-02-16
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0167-4781(91)90053-O
 Degree: -

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Title: Biochimica et Biophysica Acta-Gene Structure and Expression
  Other : Biochim. Biophys. Acta-Gene Struct. Expression
Source Genre: Journal
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Publ. Info: New York, NY : Elsevier
Pages: - Volume / Issue: 1088 (2) Sequence Number: - Start / End Page: 183 - 190 Identifier: ISSN: 0167-4781
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_1