In eukaryotes P-type ATPases are represented by a superfamily of membrane ion and lipid transporters divided into five subclasses. Substrates for classes 1-4 have been identified, however little is known about the substrate specificity of the P-type 5A and 5B transporters. Here we show that the Drosophila gene anne boleyn encodes a family of six P5B-type ATPases. Using a combination of RNAi, insertional mutagenesis, and CRISPR-Cas9 gene editing we show that some of these isoforms are required for polyamine transport and others are not. In addition, we show that the Drosophila P5A-type ATPase, encoded by CG6230 is not required for polyamine transport, indicating a different substrate specificity for this transporter sub-family. In summary, we provide evidence for the first time for an evolutionary conserved substrate specificity for the P5B-type ATPase sub-family of transporters.
If this is your thesis or dissertation, and want to learn how to access it or for more information about readership statistics, contact us at STARS@ucf.edu.
Master of Science (M.S.)
College of Sciences
Length of Campus-only Access
Masters Thesis (Open Access)
Brown, David, "A Drosophila P5B-Type ATPase is Required for Polyamine Transport" (2021). Electronic Theses and Dissertations, 2020-. 653.