Next Article in Journal
Presenilins as Drug Targets for Alzheimer’s Disease—Recent Insights from Cell Biology and Electrophysiology as Novel Opportunities in Drug Development
Next Article in Special Issue
Nitrogen Source Dependent Changes in Central Sugar Metabolism Maintain Cell Wall Assembly in Mitochondrial Complex I-Defective frostbite1 and Secondarily Affect Programmed Cell Death
Previous Article in Journal
The Influence of Selective Laser Melting (SLM) Process Parameters on In-Vitro Cell Response
Previous Article in Special Issue
Suppression of External NADPH Dehydrogenase—NDB1 in Arabidopsis thaliana Confers Improved Tolerance to Ammonium Toxicity via Efficient Glutathione/Redox Metabolism
Article Menu
Issue 6 (June) cover image

Export Article

Open AccessArticle

Decoding the Divergent Subcellular Location of Two Highly Similar Paralogous LEA Proteins

IRHS, Agrocampus-Ouest, INRA, Université d’Angers, SFR 4207 Quasav, 42 rue George Morel, 49071 Beaucouzé, France
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(6), 1620; https://doi.org/10.3390/ijms19061620
Received: 12 May 2018 / Revised: 25 May 2018 / Accepted: 28 May 2018 / Published: 31 May 2018
(This article belongs to the Special Issue Plant Mitochondria)
  |  
PDF [2518 KB, uploaded 31 May 2018]
  |  

Abstract

Many mitochondrial proteins are synthesized as precursors in the cytosol with an N-terminal mitochondrial targeting sequence (MTS) which is cleaved off upon import. Although much is known about import mechanisms and MTS structural features, the variability of MTS still hampers robust sub-cellular software predictions. Here, we took advantage of two paralogous late embryogenesis abundant proteins (LEA) from Arabidopsis with different subcellular locations to investigate structural determinants of mitochondrial import and gain insight into the evolution of the LEA genes. LEA38 and LEA2 are short proteins of the LEA_3 family, which are very similar along their whole sequence, but LEA38 is targeted to mitochondria while LEA2 is cytosolic. Differences in the N-terminal protein sequences were used to generate a series of mutated LEA2 which were expressed as GFP-fusion proteins in leaf protoplasts. By combining three types of mutation (substitution, charge inversion, and segment replacement), we were able to redirect the mutated LEA2 to mitochondria. Analysis of the effect of the mutations and determination of the LEA38 MTS cleavage site highlighted important structural features within and beyond the MTS. Overall, these results provide an explanation for the likely loss of mitochondrial location after duplication of the ancestral gene. View Full-Text
Keywords: late embryogenesis abundant protein; mitochondrion; mitochondrial import; gene duplication; paralog late embryogenesis abundant protein; mitochondrion; mitochondrial import; gene duplication; paralog
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material

SciFeed
Printed Edition Available!
A printed edition of this Special Issue is available here.

Share & Cite This Article

MDPI and ACS Style

Avelange-Macherel, M.-H.; Candat, A.; Neveu, M.; Tolleter, D.; Macherel, D. Decoding the Divergent Subcellular Location of Two Highly Similar Paralogous LEA Proteins. Int. J. Mol. Sci. 2018, 19, 1620.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top