Mitochondrial presequences are more than just address labels

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Authors: Erik Marcel Heller, Svenja Lenhard, Doron Rapaport, Johannes Herrmann
Cited by: 4
References: 125

Abstract

Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with N-terminal presequences. These presequences serve as targeting signals that facilitate the binding to mitochondrial surface receptors and translocation across the mitochondrial membranes. However, recent studies showed that presequences can be more than address tags. They can contain degradation signals recognized by components of the ubiquitin-proteasome system, and therefore, serve as timers that determine the lifespan of newly synthesized precursor proteins. Moreover, presequences can interact with components of the cytosolic chaperone system to prevent or delay precursor folding. Finally, presequences of some dually localized proteins contain targeting information not only for mitochondria but also for other cellular destinations such as the nuclear lumen or chloroplasts in plant cells. Thus, presequences contain multifaceted information to endow mitochondrial precursor proteins with specific properties that are critical for the early steps of mitochondrial protein biogenesis.

Fields of Study & Subjects

Mitochondrial Function and Pathology Photosynthetic Processes and Mechanisms Ubiquitin and proteasome pathways

Publication details

Journal / source
Protein Science
Publisher
Wiley
Volume
35
Issue
3
Pages
e70491–e70491
Publication date
12 February 2026
Language
EN