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Related Concept Videos

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Updated: Feb 24, 2026

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Acyl modification and binding of mitochondrial ACP to multiprotein complexes.

Heike Angerer1, Stefan Schönborn2, Jan Gorka2

  • 1Goethe University Frankfurt, Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Max-von-Laue Str. 9, 60438 Frankfurt, Germany.

Biochimica Et Biophysica Acta. Molecular Cell Research
|August 14, 2017
PubMed
Summary

Mitochondrial acyl carrier proteins (ACPMs) are crucial for fatty acid synthesis and complex I function. Their interaction with LYR motif proteins is vital for complex assembly and stability.

Keywords:
Cysteine desulfurase NFS1 complexFe-S cluster biogenesis, Lipoic acidMitochondrial acyl carrier proteinMitochondrial fatty acid synthesis type IIRespiratory complex I

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Area of Science:

  • Mitochondrial biology
  • Protein biochemistry
  • Enzyme complex assembly

Background:

  • Mitochondrial acyl carrier protein (ACPM/NDUFAB1) is key to fatty acid synthesis type II.
  • ACPM's role as a respiratory complex I subunit was previously unclear.
  • Yarrowia lipolytica's Complex I has two ACPMs (ACPM1, ACPM2) linked by LYRM subunits.

Purpose of the Study:

  • Investigate the function and interactions of ACPMs in yeast Complex I.
  • Elucidate the role of ACPM-LYRM interactions in complex assembly and activity.
  • Determine the structural basis for ACPM-LYRM association.

Main Methods:

  • Protein complex isolation and characterization.
  • Yeast genetics and molecular biology techniques.
  • Biochemical assays for complex I activity and assembly.

Main Results:

  • ACPM1 exists both bound to Complex I and as a free protein.
  • ACPM1 also forms complexes with LYRM4(ISD11)/NFS1 involved in Fe-S cluster biogenesis.
  • A long acyl chain on the phosphopantetheine cofactor is essential for ACPM docking to protein complexes.
  • A novel protein-protein interaction motif mediating ACPM-LYRM association is proposed.

Conclusions:

  • ACPMs have multifaceted roles beyond fatty acid synthesis, including Complex I assembly and Fe-S cluster biogenesis.
  • Specific ACPM-LYRM interactions are critical for Complex I function and stability.
  • A conserved interaction motif likely governs ACPM-LYRM binding across different protein complexes.