Abstract:
:The amino acid sequence of the mature protein of Euglena gracilis cytochrome c1 was determined by sequencing of its cDNA. A cDNA expression library was constructed from Euglena poly(A)+ RNA in phage lambda gt11 and screened with an antiserum raised against cytochrome c1 polypeptide isolated from purified E. gracilis complex III. An isolated cDNA clone consisted of 872 base pairs and encoded the mature protein with 243 amino acids. The deduced amino acid sequence contained the unusual heme binding sequence-Phe-Ala-Pro-Cys-His- (Mukai, K. et al. (1989) Eur. J. Biochem. 178, 649-656) instead of the typical sequence,-Cys-X-Y-Cys-His-, commonly found in C-type cytochromes. Comparison of the sequence with those of several other cytochromes c1 revealed that Euglena cytochrome c1 conserved the residues probably ligating heme-iron, those supposed to interact with cytochrome c and regions anchoring the mitochondrial inner membrane.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Mukai K,Wakabayashi S,Matsubara Hdoi
10.1093/oxfordjournals.jbchem.a122877subject
Has Abstractpub_date
1989-09-01 00:00:00pages
479-82issue
3eissn
0021-924Xissn
1756-2651journal_volume
106pub_type
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