The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance
The proper distribution of proteins between the cytosol and various membrane-bound compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation between protein transport machineries that translocate diverse proteins from the cytosol into these compartments and tar...
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doaj-9f2072d54ff14141b62da3351e70a81d2020-11-25T00:03:46ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2015-09-01610.3389/fphys.2015.00259159761The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevanceMarkus eKunze0Johannes eBerger1Medical University of ViennaMedical University of ViennaThe proper distribution of proteins between the cytosol and various membrane-bound compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation between protein transport machineries that translocate diverse proteins from the cytosol into these compartments and targeting signal(s) encoded within the primary sequence of these proteins that define their cellular destination. The mechanisms exerting protein translocation differ remarkably between the compartments, but the predominant targeting signals for mitochondria, chloroplasts and the ER share the N-terminal position, an α-helical structural element and the removal from the core protein by intraorganellar cleavage. Interestingly, similar properties have been described for the peroxisomal targeting signal type 2 mediating the import of a fraction of soluble peroxisomal proteins, whereas other peroxisomal matrix proteins encode the type 1 targeting signal residing at the extreme C-terminus. The structural similarity of N-terminal targeting signals poses a challenge to the specificity of protein transport, but allows the generation of ambiguous targeting signals that mediate dual targeting of proteins into different compartments. Dual targeting might represent an advantage for adaptation processes that involve a redistribution of proteins, because it circumvents the hierarchy of targeting signals. Thus, the co-existence of two equally functional import pathways into peroxisomes might reflect a balance between evolutionary constant and flexible transport routes.http://journal.frontiersin.org/Journal/10.3389/fphys.2015.00259/fullPeroxisomesspecificitysignal peptidetransit peptidePTS2Targeting signals |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Markus eKunze Johannes eBerger |
spellingShingle |
Markus eKunze Johannes eBerger The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance Frontiers in Physiology Peroxisomes specificity signal peptide transit peptide PTS2 Targeting signals |
author_facet |
Markus eKunze Johannes eBerger |
author_sort |
Markus eKunze |
title |
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance |
title_short |
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance |
title_full |
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance |
title_fullStr |
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance |
title_full_unstemmed |
The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance |
title_sort |
similarity between n-terminal targeting signals for protein import into different organelles and its evolutionary relevance |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Physiology |
issn |
1664-042X |
publishDate |
2015-09-01 |
description |
The proper distribution of proteins between the cytosol and various membrane-bound compartments is crucial for the functionality of eukaryotic cells. This requires the cooperation between protein transport machineries that translocate diverse proteins from the cytosol into these compartments and targeting signal(s) encoded within the primary sequence of these proteins that define their cellular destination. The mechanisms exerting protein translocation differ remarkably between the compartments, but the predominant targeting signals for mitochondria, chloroplasts and the ER share the N-terminal position, an α-helical structural element and the removal from the core protein by intraorganellar cleavage. Interestingly, similar properties have been described for the peroxisomal targeting signal type 2 mediating the import of a fraction of soluble peroxisomal proteins, whereas other peroxisomal matrix proteins encode the type 1 targeting signal residing at the extreme C-terminus. The structural similarity of N-terminal targeting signals poses a challenge to the specificity of protein transport, but allows the generation of ambiguous targeting signals that mediate dual targeting of proteins into different compartments. Dual targeting might represent an advantage for adaptation processes that involve a redistribution of proteins, because it circumvents the hierarchy of targeting signals. Thus, the co-existence of two equally functional import pathways into peroxisomes might reflect a balance between evolutionary constant and flexible transport routes. |
topic |
Peroxisomes specificity signal peptide transit peptide PTS2 Targeting signals |
url |
http://journal.frontiersin.org/Journal/10.3389/fphys.2015.00259/full |
work_keys_str_mv |
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