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N-glycoproteins exhibit a positive expression level-evolutionary rate correlation.

Felix Feyertag1, Patricia M Berninsone1, David Alvarez-Ponce1

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Highly expressed proteins usually evolve slowly, but N-glycosylated proteins show the opposite trend. N-linked glycosylation in secreted proteins reverses the typical expression level-evolutionary rate anticorrelation.

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E-R anticorrelationN-linked glycosylationdN/dSrates of evolution

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Protein evolution rates vary significantly, influenced by expression levels.
  • The expression level-evolutionary rate (E-R) anticorrelation is linked to misfolding and misinteraction costs.
  • Secreted proteins exhibit a weaker or absent E-R anticorrelation.

Purpose of the Study:

  • To investigate the impact of N-linked glycosylation on the E-R anticorrelation in secreted proteins.
  • To determine if N-glycosylation modifies the evolutionary rate of highly expressed proteins.

Main Methods:

  • Analysis of protein sequences and expression data.
  • Comparative evolutionary rate analysis of N-glycosylated versus non-N-glycosylated secreted proteins.
  • Statistical assessment of the E-R correlation in different protein subsets.

Main Results:

  • N-glycosylated secreted proteins display a positive E-R correlation.
  • Highly expressed N-glycoproteins evolve faster than lowly expressed ones.
  • This finding contrasts with the typical E-R anticorrelation observed in intracellular proteins.

Conclusions:

  • N-linked glycosylation significantly alters the evolutionary dynamics of secreted proteins.
  • The strong quality control on N-glycoproteins may lead to faster evolution despite high expression.
  • This suggests a unique evolutionary mechanism for N-glycosylated secreted proteins.