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Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
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Selectivity of aggregation-determining interactions.

Ashok Ganesan1, Maja Debulpaep2, Hannah Wilkinson1

  • 1VIB Switch Laboratory, VIB, B-3000 Leuven, Belgium; Department of Cellular and Molecular Medicine, KU Leuven, B-3000 Leuven, Belgium.

Journal of Molecular Biology
|December 3, 2014
PubMed
Summary
This summary is machine-generated.

Protein aggregation is highly specific, with unique sequences driving self-assembly. This selectivity explains why protein clumps in cells are homogeneous, even with many aggregation-prone proteins present.

Keywords:
amyloiddetectioninteractionprotein aggregationspecificity

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Protein aggregation is sequence-specific, favoring self-assembly over cross-seeding.
  • The homogeneity of protein inclusions in vivo is surprising given the abundance of aggregation-prone proteins.

Purpose of the Study:

  • Investigate the selectivity of protein aggregation within a proteomic context.
  • Compare aggregation-determined interactions with antibody binding specificity.

Main Methods:

  • Synthesized biotin-labeled peptides from aggregation-determining sequences of β-galactosidase, C-reactive protein, and prostate-specific antigen.
  • Analyzed peptide interactions in E. coli lysate, human serum, and seminal plasma using a Western blot-like assay.
  • Utilized spectroscopic and mutagenic studies to confirm binding interactions.

Main Results:

  • Observed specific peptide accumulation in bands identical to antibody staining.
  • Confirmed peptide accumulation resulted from binding to identical sequences on immobilized target proteins.
  • Found approximately 90% of aggregating sequences are unique within their respective proteomes.

Conclusions:

  • The specificity and low sequence redundancy of aggregating sequences contribute to homogeneous protein aggregation in vivo.
  • Intrinsic proteomic properties naturally compartmentalize aggregation events in sequence space.
  • This specificity may aid cellular response to proteostatic stress by focusing chaperone activity.