Drosophila delta-1-pyrroline-5-carboxylate dehydrogenase (P5CDh) is required for proline breakdown and mitochondrial integrity-Establishing a fly model for human type II hyperprolinemia

Authors

Fang He, Louisiana State University
Patrick J. DiMario, Louisiana State University

Document Type

Article

Publication Date

5-1-2011

Abstract

Delta-1-pyrroline-5-carboxylate dehydrogenase (P5CDh) is a nuclear-encoded mitochondrial enzyme that catalyzes the second step in proline degradation. Mutations in human P5CDh cause type II hyperprolinemia, a complex syndrome displaying increased serum proline and mental disabilities. Conceptual gene CG7145 in Drosophila melanogaster encodes the orthologous DmP5CDh1. The mutant allele CG7145^f04633 contains a piggyBac transposon that truncates the enzyme by 83 residues. Heterozygous (CG7145^f04633/TM3) individuals developed normally, while homozygous (CG7145^f04633/CG7145^f04633) individuals displayed proline levels twice that of normal, swollen mitochondria, and ultimately larval and pupal lethality. We believe this is the first correlation between the loss of P5CDh and morphological defects in mitochondria. © 2010 Elsevier B.V. and Mitochondria Research Society.

Publication Source (Journal or Book title)

Mitochondrion

First Page

397

Last Page

404

Recommended Citation

He, F., & DiMario, P. (2011). Drosophila delta-1-pyrroline-5-carboxylate dehydrogenase (P5CDh) is required for proline breakdown and mitochondrial integrity-Establishing a fly model for human type II hyperprolinemia. Mitochondrion, 11 (3), 397-404. https://doi.org/10.1016/j.mito.2010.12.001