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    Acetylation

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Flag for inappropriate content
    15 views2 pages

    Acetylation

    Uploaded by

    Steven4654
    Acetylation

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Flag for inappropriate content
    of 2

    Acetylation

    Introduction
    Acetylation is an important modification of proteins in cell biology. N-acetylation, or the
    transfer of an acetyl group to nitrogen, occurs in almost all eukaryotic proteins through both
    irreversible and reversible mechanisms. N-terminal acetylation requires the cleavage of the N-
    terminal methionine by methionine aminopeptidase (MAP) before replacing the amino acid
    with an acetyl group from acetyl-CoA by N-acetyltransferase (NAT) enzymes. It occurs as a
    co-translational and post-translational modification of proteins, for example, histones, STAT,
    and microtubules. Acetylation modification regulates protein conformation, and dysfunction of
    this modification has been implied in many diseases, including cancer. This type of
    acetylation is co-translational, in that N-terminus is acetylated on growing polypeptide chains
    that are still attached to the ribosome. While 80-90% of eukaryotic proteins are acetylated in
    this manner, the exact biological significance is still unclear.

    N-terminal Acetylation
    N-acetylation, or the transfer of an acetyl group to nitrogen, occurs in almost all eukaryotic
    proteins through both irreversible and reversible mechanisms. N-terminal acetylation requires
    the cleavage of the N-terminal methionine by methionine aminopeptidase (MAP) before
    replacing the amino acid with an acetyl group from acetyl-CoA by N-acetyltransferase (NAT)
    enzymes. This type of acetylation is co-translational, in that N-terminus is acetylated on
    growing polypeptide chains that are still attached to the ribosome. While 80-90% of eukaryotic
    proteins are acetylated in this manner, the exact biological significance is still unclear.

    Lysine Acetylation - Regulation of Histone


    Acetylation at the ε-NH2 of lysine (termed lysine acetylation) on histone N-termini is a
    common method of regulating gene transcription. Histone acetylation is a reversible event
    that reduces chromosomal condensation to promote transcription, and the acetylation of
    these lysine residues is regulated by transcription factors that contain histone
    acetyletransferase (HAT) activity. While transcription factors with HAT activity act as
    transcription co-activators, histone deacetylase (HDAC) enzymes are co-repressors that
    reverse the effects of acetylation by reducing the level of lysine acetylation and increasing
    chromosomal condensation. While acetylation was first detected in histones, cytoplasmic
    proteins have been reported to also be acetylated, and therefore acetylation seems to play a
    greater role in cell biology than simply transcriptional regulation. Furthermore, crosstalk
    between acetylation and other post-translational modifications,
    including phosphorylation, ubiquitination and methylation, can modify the biological function of
    the acetylated protein.
    Creative Proteomics has established a highly sensitive HPLC-MS/MS platform that can
    analyze acetylation in multiple samples and in both eukaryotic and prokaryotic organisms. In
    addition, we have optimized our protocol to enable more fast and sensitive site mapping
    service for acetylation analysis.

    Workflow of our Acetylation analysis service:


     In gel or in solution digestion of proteins
     Enrichment of acetylated proteins by antibodies targeting specific acetylation motifs (optional
    step)
     HPLC separation, followed by ESI-TOF MS/MS analysis
     Mass spectrometry data interpretation
    Technology platform:
     Ion Chromatography
     High Performance Liquid Chromatography (HPLC)
     Matrix Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS)
    Creative Proteomics also provide the following bioinformatics services in Protein Post-
    translational Modification Analysis:
    Functional annotation and enrichment analysis
    Clustering analysis
    Network analysis
    Statistical analysis
    Proteomic analysis of post-translational modifications
    Please feel free to Contact Us to discuss your projects. We hope you will find that we can
    meet your research needs.

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