Faculty Publications

An In Silico Analysis Of Cytochrome C From Phanerochaete Chrysosporium: Its Amino Acid Sequence And Characterization Of Gene Structural Elements

Document Type

Article

Keywords

Amino acid sequence, Biodegradation, Cytochrome c, Fungi, Gene, Lignin, Lignin peroxidases, Phanerochaete chrysosporium, White rot fungi

Journal/Book/Conference Title

In Silico Biology

Volume

8

Issue

1

First Page

1

Last Page

13

Abstract

An in silico approach was used to investigate cytochrome c and the cytochrome c gene of Phanerochaete chrysosporium. The cytochrome c gene contains four introns. Omission of the introns reveals a DNA sequence coding for a complete predicted amino acid sequence for P. chrysosporium cytochrome c consistent with those of other cytochromes c. Fungal cytochromes c often have a short N-terminal peptide preceding a Gly that is the N-terminal amino acid in many cytochromes c. Thus a microexon codes for an N-terminal pentapeptide (MetProTyrAlaPro) in P. chrysosporium that is identical to the N-terminal pentapeptide of Schizosaccharomyces pombe, a well studied yeast, the genome of which bears more similarity to higher eukaryotes than to other fungi. The fourth intron, when omitted, reveals the presence of another microexon resulting in a sequence for the C-terminal portion of the protein and the stop codon. Interestingly, two interpretations for the sequence of this intron leads to predictions that the C-terminal sequence ends with either AlaValAsn or AlaTyr. Selected aspects of the molecular architecture of cytochrome c and regulatory control elements of the P. chrysosporium cytochrome c gene were analyzed and compared to those present in other fungi and to those present in genes for lignin peroxidases and cytochromes P-450, two important families of hemeproteins produced by this fungus. © 2008 IOS Press. All rights reserved.

Department

Department of Chemistry and Biochemistry

Original Publication Date

5-1-2008

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