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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

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Tools to tackle protein acetylation

Kinga Kamieniarz1, Robert Schneider

  • 1MPI of Immunobiology, Stübeweg 51, 79108 Freiburg, Germany.

Chemistry & Biology
|October 31, 2009
PubMed

Abstract:

In the recent issue of Molecular Cell, Neumann et al. dissect the effect of H3K56 acetylation on chromatin structure using a novel method for generation of acetylated proteins. This is a valuable addition to the toolkit for those interested in unraveling how posttranslational modifications regulate protein function.

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...

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