Hello tedmccall-ga,
You asked: ?I would like to know what i could find in this article.?
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http://scholar.google.com/scholar?q=Bacterial+expression+of+a+mitochondrial+cytochrome+&ie=UTF-8&oe=UTF-8&hl=en
Search Results for: Bacterial expression of a mitochondrial cytochrome
The citation from PubMed includes a fairly long abstract that gives
you an excellent summary of what you will find in this article. You
could take any topic that appeals to you from this article abstract
and do a new search of either Google Scholar or of PubMed and work
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Best wishes for your research project.
~ czh ~
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9558351&dopt=Citation
NOTE: Performing your original search, Bacterial expression of a
mitochondrial cytochrome , in PubMed will retrieve 91 citations.
PMID: 9558351 [PubMed - indexed for MEDLINE]
Biochemistry. 1998 Apr 28;37(17):6124-31.
Bacterial expression of a mitochondrial cytochrome c. Trimethylation
of lys72 in yeast iso-1-cytochrome c and the alkaline conformational
transition.
Pollock WB, Rosell FI, Twitchett MB, Dumont ME, Mauk AG.
Department of Biochemistry and Molecular Biology, University of
British Columbia, Vancouver, Canada.
Saccharomyces cerevisiae iso-1-cytochrome c has been expressed in
Escherichia coli by coexpression of the genes encoding the cytochrome
(CYC1) and yeast cytochrome c heme lyase (CYC3). Construction of this
expression system involved cloning the two genes in parallel into the
vector pUC18 to give the plasmid pBPCYC1(wt)/3. Transcription was
directed by two promoters, Lac and Trc, that were located upstream
from CYC1. Both proteins were expressed in the cytoplasm of E. coli
cells harboring the plasmid. Semianaerobic cultures grown in a
fermentor produced 15 mg of recombinant iso-1-cytochrome c per liter
of culture. Attempts to increase production by addition of IPTG
suppressed the number of copies of the CYC1 gene within the
population. Wild-type iso-1-cytochrome c expressed with pBPCYC1(wt)/3
in E. coli was compared to the same protein expressed in yeast. At
neutral pH, the two proteins exhibit indistinguishable spectroscopic
and physical (Tm, Em') characteristics. However, electrospray mass
spectrometry revealed that the lysyl residue at position 72 is not
trimethylated by E. coli as it is by S. cerevisiae. Interestingly, the
pKa of the alkaline transition of the protein expressed in E. coli is
approximately 0.6 pKa unit lower than that observed for the cytochrome
expressed in yeast (8.5-8.7). 1H NMR spectroscopy of the bacterially
expressed cytochrome collected at high pH revealed the presence of a
third alkaline conformer that is not observed in the corresponding
spectrum of the cytochrome expressed in yeast. These observations
suggest that Lys72 can serve as an axial ligand to the heme iron of
alkaline iso-1-ferricytochrome c if it is not modified
posttranscriptionally to trimethyllysine.
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