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The structure and expression of cytochrome b(5) in Drosophila

Kula, Maureen Elizabeth
http://rave.ohiolink.edu/etdc/view?acc_num=case1058215222

Abstract Details

1995, Doctor of Philosophy, Case Western Reserve University, Biology.
Our laboratory has identified and characterized in Drosophila melanogaster a unique gene that represents a putative nuclear encoded form of cytochrome b5 (Cyt-b). The Cyt-b locus is in close proximity to the myosin heavy chain gene (Mhc) at 36B on the second chromosome, and the two genes are convergently transcribed. The coding sequence of Cyt-b is 1242 nucleotides in length which translates into a 414 amino acid protein with a predicted molecular weight of 47 kilodaltons. Cyt-b is a single copy gene that is expressed as a single mRNA throughout development and may be co-expressed with Mhc (Levin, et al., 1989). I have examined the evolutionary conservation of this locus by comparing the Cyt-b genes of two species of Drosophila. Cyt-b is highly conserved in Drosophila melanogaster and Drosophila virilis. Although the genetic structures of these homologues differ, the putative Cyt-b proteins of Drosophila melanogaster and Drosophila virilis are over 75% identical, and the greatest levels of homology are observed in areas of potential importance for protein structure and function (Kula, et al., 1994). Inspection of the Cyt-b protein sequence reveals that it is related to the b-type cytochromes containing specifically a consensus b5 heme-binding domain, and this protein contains a mitochondrial targeting sequence. Considering the hi storical residence of Drosophila cytochrome b encoding sequences solely in the mitochondrial genome (Clary and Wolstenholme, 1985; Garesse, 1988), the prospect of Cyt-b representing a nuclear-encoded b-type cytochrome is intriguing. I have used an antibody directed against the Drosophila melanogaster Cyt-b to determine various protein characteristics. This analysis validates many of the predictions made about the putative Cyt-b protein product from analysis of the amino acid sequence. Evidence indicates that this protein is expressed throughout development and is translocated to the mitochondria.
Charles Rozek (Advisor)
207 p.
Biology, Molecular
cytochrome b(5) Drosophila

Recommended Citations

Citations

  • Kula, M. E. (1995). The structure and expression of cytochrome b(5) in Drosophila [Doctoral dissertation, Case Western Reserve University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=case1058215222

    APA Style (7th edition)

  • Kula, Maureen. The structure and expression of cytochrome b(5) in Drosophila. 1995. Case Western Reserve University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=case1058215222.

    MLA Style (8th edition)

  • Kula, Maureen. "The structure and expression of cytochrome b(5) in Drosophila." Doctoral dissertation, Case Western Reserve University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=case1058215222

    Chicago Manual of Style (17th edition)

case1058215222
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© 1995, all rights reserved.
This open access ETD is published by Case Western Reserve University School of Graduate Studies and OhioLINK.