Dataset Information

Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.

ABSTRACT: In plants, the voltage-dependent anion-selective channel (VDAC) is a major component of a pathway involved in transfer RNA (tRNA) translocation through the mitochondrial outer membrane. However, the way in which VDAC proteins interact with tRNAs is still unknown. Potato mitochondria contain two major mitochondrial VDAC proteins, VDAC34 and VDAC36. These two proteins, composed of a N-terminal ?-helix and of 19 ?-strands forming a ?-barrel structure, share 75% sequence identity. Here, using both northwestern and gel shift experiments, we report that these two proteins interact differentially with nucleic acids. VDAC34 binds more efficiently with tRNAs or other nucleic acids than VDAC36. To further identify specific features and critical amino acids required for tRNA binding, 21 VDAC34 mutants were constructed and analyzed by northwestern. This allowed us to show that the ?-barrel structure of VDAC34 and the first 50 amino acids that contain the ?-helix are essential for RNA binding. Altogether the work shows that during evolution, plant mitochondrial VDAC proteins have diverged so as to interact differentially with nucleic acids, and this may reflect their involvement in various specialized biological functions.

SUBMITTER: Salinas T

PROVIDER: S-EPMC4150812 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.

Salinas Thalia T El Farouk-Ameqrane Samira S Ubrig Elodie E Sauter Claude C Duchêne Anne-Marie AM Maréchal-Drouard Laurence L

Nucleic acids research 20140811 15

In plants, the voltage-dependent anion-selective channel (VDAC) is a major component of a pathway involved in transfer RNA (tRNA) translocation through the mitochondrial outer membrane. However, the way in which VDAC proteins interact with tRNAs is still unknown. Potato mitochondria contain two major mitochondrial VDAC proteins, VDAC34 and VDAC36. These two proteins, composed of a N-terminal α-helix and of 19 β-strands forming a β-barrel structure, share 75% sequence identity. Here, using both n ...[more]

PMID: 25114051

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Dataset Information

Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.

Publications

Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.

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