A direct role for a mitochondrial targeting sequence in signalling stress.

ABSTRACT: Mitochondrial protein import is required for maintaining organellar function¹. Perturbations in this process are associated with various physiological and disease conditions². Several stress responses, including the mitochondrial compromised protein import response (mitoCPR), combat damage caused by mitochondrial protein import defects². However, how this defect is sensed remains largely unknown. Here we reveal that the conserved mitochondrial Hsp70 co-chaperone, Mge1, acts as a stress messenger in budding yeast. During mitochondrial stress, unimported Mge1 entered the nucleus and triggered the transcription of mitoCPR target genes. This was mediated by the interaction of Mge1 with the transcription factor Pdr3 on DNA regulatory elements. The mitochondrial

SUBMITTER: Yuan Z 

PROVIDER: S-EPMC7618714 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature