Andreas Carlström

ORCID: 0000-0001-6159-8753
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About
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Research Areas
  • Mitochondrial Function and Pathology
  • RNA and protein synthesis mechanisms
  • Photosynthetic Processes and Mechanisms
  • Protein Structure and Dynamics
  • ATP Synthase and ATPases Research
  • RNA modifications and cancer
  • Enzyme Structure and Function
  • Microbial Metabolic Engineering and Bioproduction
  • Adipose Tissue and Metabolism
  • Cancer, Hypoxia, and Metabolism
  • Exercise and Physiological Responses
  • Metabolomics and Mass Spectrometry Studies
  • RNA Research and Splicing
  • Biotin and Related Studies
  • Cardiovascular and exercise physiology
  • Hemoglobin structure and function
  • Muscle metabolism and nutrition
  • Ubiquitin and proteasome pathways

University of Gothenburg
2024-2025

Stockholm University
2018-2024

Mitochondria contain their own gene expression systems, including membrane-bound ribosomes dedicated to synthesizing a few hydrophobic subunits of the oxidative phosphorylation (OXPHOS) complexes. We used proximity-dependent biotinylation technique, BioID, coupled with mass spectrometry delineate in baker’s yeast comprehensive network factors involved biogenesis mitochondrial encoded proteins. This (MiGENet) encompasses proteins transcription, RNA processing, translation, or protein...

10.1016/j.molcel.2020.07.024 article EN cc-by Molecular Cell 2020-09-01

Folding of newly synthesized proteins poses challenges for a functional proteome. Dedicated protein quality control (PQC) systems either promote the folding nascent polypeptides at ribosomes or, if this fails, ensure their degradation. Although well studied cytosolic biogenesis, it is not understood how these processes work mitochondrially encoded proteins, key subunits oxidative phosphorylation (OXPHOS) system. Here, we identify dedicated hubs in proximity to mitoribosomal tunnel exits...

10.1016/j.molcel.2023.09.001 article EN cc-by Molecular Cell 2023-09-25

Mitochondrial gene expression is essential for oxidative phosphorylation. Mitochondrial-encoded mRNAs are translated by dedicated mitochondrial ribosomes (mitoribosomes), whose regulation remains elusive. In the baker's yeast Saccharomyces cerevisiae , nuclear-encoded translational activators (TAs) facilitate transcript-specific translation a yet unknown mechanism. Here, we investigated function of TAs containing RNA-binding pentatricopeptide repeats (PPRs) using selective mitoribosome...

10.1101/2025.01.26.634913 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2025-01-26

Mitochondrial gene expression needs to be balanced with cytosolic translation produce oxidative phosphorylation complexes. In yeast, translational feedback loops involving lowly expressed proteins called activators help achieve this balance. Synthesis of cytochrome b (Cytb or COB), a core subunit complex III in the respiratory chain, is controlled by three and assembly factor Cbp3-Cbp6. However, molecular interface between COB loop yet unknown. Here, using protein-proximity mapping combined...

10.1101/2025.01.30.635641 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2025-01-31

Mitochondrial gene expression in Saccharomyces cerevisiae is responsible for the production of highly hydrophobic subunits oxidative phosphorylation system. Membrane insertion occurs cotranslationally on membrane-bound mitochondrial ribosomes. Here, by employing a systematic mass spectrometry–based approach, we discovered previously uncharacterized membrane protein Mrx15 that interacts via soluble C-terminal domain with large ribosomal subunit. contacts translation products during their...

10.1091/mbc.e18-04-0227 article EN cc-by-nc-sa Molecular Biology of the Cell 2018-08-09

Assembly of the mitochondrial respiratory chain requires coordinated synthesis and nuclear encoded subunits, redox co-factor acquisition, correct joining subunits to form functional complexes. The conserved Cbp3–Cbp6 chaperone complex binds newly synthesized cytochrome <i>b</i> supports ordered acquisition heme co-factors. Moreover, it functions as a translational activator by interacting with mitoribosome. Cbp3 consists two distinct domains: an N-terminal domain present in homologs highly...

10.1074/jbc.ra119.010483 article EN cc-by Journal of Biological Chemistry 2019-09-20

The mitochondrial proteome contains proteins from two different genetic systems. Proteins are either synthesized in the cytosol and imported into compartments of organelle or directly produced matrix. To ensure proteostasis, monitored by quality control system, which will degrade non-native polypeptides. Defective membrane degraded membrane-bound AAA-proteases. These proteases regulated factors promoting protein turnover preventing their degradation. Here we determined interactions between...

10.3390/cells7100172 article EN cc-by Cells 2018-10-17

Membrane proteins carrying redox cofactors are key subunits of respiratory chain complexes, yet the exact path their folding and maturation remains poorly understood. Here, using cryo-EM structure prediction via Alphafold2, we generated models early assembly intermediates cytochrome b (Cytb), a central subunit complex III. The predicted first intermediate suggests how binding Cytb to factor Cbp3-Cbp6 imposes an open configuration facilitate acquisition its heme cofactors. Moreover,...

10.1002/1873-3468.14888 article EN cc-by FEBS Letters 2024-04-25

ABSTRACT The mitochondrial respiratory chain (MRC) enzymatic complexes, essential for aerobic energy transduction in eukaryotic cells, are organized into evolutionarily conserved higher-order structures known as supercomplexes (SCs). elucidation of the physiological relevance SCs is our understanding function and cellular bioenergetics, yet it has been severely hampered by limited availability experimental models isolating SC formation sole variable. In yeast Saccharomyces cerevisiae , where...

10.1101/2024.12.19.629262 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-12-21
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