» Articles » PMID: 29593233

Mechanism of Translation Control of the Alternative Drosophila Melanogaster Voltage Dependent Anion-selective Channel 1 MRNAs

Overview
Journal Sci Rep
Specialty Science
Date 2018 Mar 30
PMID 29593233
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

The eukaryotic porin, also called the Voltage Dependent Anion-selective Channel (VDAC), is the main pore-forming protein of the outer mitochondrial membrane. In Drosophila melanogaster, a cluster of genes evolutionarily linked to VDAC is present on chromosome 2L. The main VDAC isoform, called VDAC1 (Porin1), is expressed from the first gene of the cluster. The porin1 gene produces two splice variants, 1A-VDAC and 1B-VDAC, with the same coding sequence but different 5' untranslated regions (UTRs). Here, we studied the influence of the two 5' UTRs, 1A-5' UTR and 1B-5' UTR, on transcription and translation of VDAC1 mRNAs. In porin-less yeast cells, transformation with a construct carrying 1A-VDAC results in the expression of the corresponding protein and in complementation of a defective cell phenotype, whereas the 1B-VDAC sequence actively represses VDAC expression. Identical results were obtained using constructs containing the two 5' UTRs upstream of the GFP reporter. A short region of 15 nucleotides in the 1B-5' UTR should be able to pair with an exposed helix of 18S ribosomal RNA (rRNA), and this interaction could be involved in the translational repression. Our data suggest that contacts between the 5' UTR and 18S rRNA sequences could modulate the translation of Drosophila 1B-VDAC mRNA. The evolutionary significance of this finding is discussed.

Citing Articles

Developing a Novel and Optimized Yeast Model for Human VDAC Research.

Baranek-Grabinska M, Grabinski W, Musso D, Karachitos A, Kmita H Int J Mol Sci. 2024; 25(23).

PMID: 39684721 PMC: 11641349. DOI: 10.3390/ijms252313010.


Sperm epigenetics and sperm RNAs as drivers of male infertility: truth or myth?.

Leggio L, Paterno G, Cavallaro F, Falcone M, Vivarelli S, Manna C Mol Cell Biochem. 2024; 480(2):659-682.

PMID: 38717684 PMC: 11835981. DOI: 10.1007/s11010-024-04962-w.


VDAC1 Knockout Affects Mitochondrial Oxygen Consumption Triggering a Rearrangement of ETC by Impacting on Complex I Activity.

Magri A, Cubisino S, Battiato G, Lipari C, Conti Nibali S, Saab M Int J Mol Sci. 2023; 24(4).

PMID: 36835102 PMC: 9963415. DOI: 10.3390/ijms24043687.


Extracellular Vesicles as Novel Diagnostic and Prognostic Biomarkers for Parkinson's Disease.

Leggio L, Paterno G, Vivarelli S, Falzone G, Giachino C, Marchetti B Aging Dis. 2021; 12(6):1494-1515.

PMID: 34527424 PMC: 8407885. DOI: 10.14336/AD.2021.0527.


Small Hexokinase 1 Peptide against Toxic SOD1 G93A Mitochondrial Accumulation in ALS Rescues the ATP-Related Respiration.

Magri A, Risiglione P, Caccamo A, Formicola B, Tomasello M, Arrigoni C Biomedicines. 2021; 9(8).

PMID: 34440152 PMC: 8392704. DOI: 10.3390/biomedicines9080948.


References
1.
Kouba T, Rutkai E, Karaskova M, Valasek L . The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes. Nucleic Acids Res. 2011; 40(6):2683-99. PMC: 3315329. DOI: 10.1093/nar/gkr1083. View

2.
Linden M, Karlsson G . Identification of porin as a binding site for MAP2. Biochem Biophys Res Commun. 1996; 218(3):833-6. DOI: 10.1006/bbrc.1996.0148. View

3.
Aiello R, Messina A, Schiffler B, Benz R, Tasco G, Casadio R . Functional characterization of a second porin isoform in Drosophila melanogaster. DmPorin2 forms voltage-independent cation-selective pores. J Biol Chem. 2004; 279(24):25364-73. DOI: 10.1074/jbc.M310572200. View

4.
Shimizu S, Narita M, Tsujimoto Y . Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature. 1999; 399(6735):483-7. DOI: 10.1038/20959. View

5.
Pastorino J, Hoek J . Regulation of hexokinase binding to VDAC. J Bioenerg Biomembr. 2008; 40(3):171-82. PMC: 2662512. DOI: 10.1007/s10863-008-9148-8. View