Keywords

Drosophila; P5B-type ATPase; Polyamine transport; Gene editing; Substrate specificity

Abstract

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.

Notes

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Graduation Date

2021

Semester

Summer

Advisor

Vonkalm, Laurence

Degree

Master of Science (M.S.)

College

College of Sciences

Department

Biology

Degree Program

Biology

Format

application/pdf

Identifier

CFE0008624;DP0025355

URL

https://purls.library.ucf.edu/go/DP0025355

Language

English

Release Date

August 2021

Length of Campus-only Access

None

Access Status

Masters Thesis (Open Access)

Subjects

Adenosine triphosphatase genes; Polyamines--Metabolism; Biological transport, Active--Research; Drosophila melanogaster--Physiology; Membrane proteins--Physiological transport

Included in

Biology Commons

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