---
pmid: '21130726'
title: 'A novel subfamily of mitochondrial dicarboxylate carriers from Drosophila
  melanogaster: biochemical and computational studies.'
authors:
- Iacopetta D
- Madeo M
- Tasco G
- Carrisi C
- Curcio R
- Martello E
- Casadio R
- Capobianco L
- Dolce V
journal: Biochim Biophys Acta
year: '2011'
full_text_available: false
doi: 10.1016/j.bbabio.2010.11.013
pubmed_publication_types:
- Journal Article
publication_type: PRIMARY_RESEARCH
---

# A novel subfamily of mitochondrial dicarboxylate carriers from Drosophila melanogaster: biochemical and computational studies.
**Authors:** Iacopetta D, Madeo M, Tasco G, Carrisi C, Curcio R, Martello E, Casadio R, Capobianco L, Dolce V
**Journal:** Biochim Biophys Acta (2011)
**DOI:** [10.1016/j.bbabio.2010.11.013](https://doi.org/10.1016/j.bbabio.2010.11.013)

## Abstract

1. Biochim Biophys Acta. 2011 Mar;1807(3):251-61. doi:
10.1016/j.bbabio.2010.11.013. Epub 2010 Dec 3.

A novel subfamily of mitochondrial dicarboxylate carriers from Drosophila
melanogaster: biochemical and computational studies.

Iacopetta D(1), Madeo M, Tasco G, Carrisi C, Curcio R, Martello E, Casadio R,
Capobianco L, Dolce V.

Author information:
(1)Department of Pharmaco-Biology, University of Calabria, Arcavacata di Rende,
87036 Cosenza, Italy.

The dicarboxylate carrier is an important member of the mitochondrial carrier
family, which catalyzes an electroneutral exchange across the inner
mitochondrial membrane of dicarboxylates for inorganic phosphate and certain
sulfur-containing compounds. Screening of the Drosophila melanogaster genome
revealed the presence of a mitochondrial carrier subfamily constituted by four
potential homologs of mammalian and yeast mitochondrial dicarboxylate carriers
designated as DmDic1p, DmDic2p, DmDic3p, and DmDic4p. In this paper, we report
that DmDIC1 is broadly expressed at comparable levels in all development stages
investigated whereas DmDIC3 and DmDIC4 are expressed only in the pupal stage, no
transcripts are detectable for DmDIC2. All expressed proteins are localized in
mitochondria. The transport activity of DmDic1-3-4 proteins has been
investigated by reconstitution of recombinant purified protein into liposomes.
DmDic1p is a typical dicarboxylate carrier showing similar substrate specificity
and inhibitor sensitivity as mammalian and yeast mitochondrial dicarboxylate
carriers. DmDic3p seems to be an atypical dicarboxylate carrier being able to
transport only inorganic phosphate and certain sulfur-containing compounds. No
transport activity was observed for DmDic4p. The biochemical results have been
supported at molecular level by computing the protein structures and by
structural alignments. All together these results indicate that D. melanogaster
dicarboxylate carriers form a protein subfamily but the modifications in the
amino acids sequences are indicative of specialized functions.

Copyright © 2010 Elsevier B.V. All rights reserved.

DOI: 10.1016/j.bbabio.2010.11.013
PMID: 21130726 [Indexed for MEDLINE]