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N-Terminal Methionine Processing.

Paul T Wingfield1

  • 1Protein Expression Laboratory, NIAMS/NIH, Bethesda, Maryland.

Current Protocols in Protein Science
|April 4, 2017
PubMed
Summary
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The enzyme methionine aminopeptidase (MAP) cleaves initiating methionine from proteins. This cleavage is predictable based on the size of the adjacent amino acid residue, aiding recombinant protein expression.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Protein synthesis initiates with methionine in eukaryotes and formylmethionine in prokaryotes.
  • N-terminal methionine can be removed post-translationally by methionine aminopeptidase (MAP).
  • Understanding methionine cleavage is crucial for recombinant protein production.

Purpose of the Study:

  • To identify a universal rule predicting methionine aminopeptidase (MAP) processing of N-terminal methionine.
  • To correlate the size of the penultimate residue with MAP cleavage activity.

Main Methods:

  • Analysis of N-terminal sequences of proteins expressed in bacterial and mammalian systems.
  • Correlation of the radius of gyration of penultimate amino acid side chains with methionine cleavage.
Keywords:
N-terminal methionineexopeptidase activitymethionine aminopepidasesprotein synthesis

Related Experiment Videos

Main Results:

  • A simple rule predicts MAP processing based on the penultimate residue.
  • Methionine is cleaved if the penultimate residue's side chain has a radius of gyration ≤ 1.29 Å.

Conclusions:

  • The size of the penultimate amino acid is a key determinant of N-terminal methionine cleavage by MAP.
  • This rule provides a predictable framework for managing methionine processing in recombinant protein expression.