Response to Comment on "Protein assemblies ejected directly from native membranes yield complexes for mass...

Area of Science:

• Biochemistry
• Molecular Biology
• Cell Biology

Background:

• Mitochondrial membrane protein complexes play crucial roles in cellular respiration.
• Understanding the structural integrity of these complexes upon isolation is vital.
• Previous studies have presented conflicting data regarding protein complex stability.

Purpose of the Study:

• To provide further evidence supporting the assignments of mitochondrial protein complexes.
• To address claims of protein degradation and incorrect assignments in prior research.
• To validate the structural integrity of protein complexes ejected from mitochondrial membranes.

Main Methods:

• Utilizing advanced biochemical assays to analyze protein complexes.
• Employing mass spectrometry for accurate protein identification and quantification.
• Comparing experimental results with established "native states" obtained in detergent micelles.

Main Results:

• All identified mitochondrial protein complexes were ejected either intact or as known intermediate states.
• Core subunit interactions within the complexes were consistently maintained.
• No evidence of protein degradation or rearrangement was observed, contradicting previous claims.

Conclusions:

• The findings strongly support the initial assignments of mitochondrial protein complexes.
• The structural integrity of these complexes is maintained upon ejection from mitochondrial membranes.
• The study refutes claims of degradation and incorrect assignments, reinforcing the validity of the experimental approach.