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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.
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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Published on: January 8, 2018

Protein N-acylation overrides differing targeting signals.

Simon Stael1, Roman G Bayer1, Norbert Mehlmer1

  • 1Department of Biochemistry and Cell Biology, MFPL, University of Vienna. Dr. Bohrgasse 9, A-1030 Vienna, Austria.

FEBS Letters
|January 12, 2011
PubMed
Summary

Protein acylation, specifically N-myristoylation, impacts protein targeting predictions. Modifying acylation can redirect protein kinases and other proteins to chloroplasts or the nucleus.

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Area of Science:

  • * Molecular Biology
  • * Bioinformatics
  • * Plant Cell Biology

Background:

  • * Accurate prediction of protein localization is crucial for understanding cellular function.
  • * Existing bioinformatics tools often mispredict chloroplast localization for protein kinases.
  • * N-terminal protein acylation, particularly N-myristoylation, plays a significant role in protein targeting and function.

Purpose of the Study:

  • * To investigate the role of N-terminal protein acylation in the misprediction of chloroplast localization for protein kinases.
  • * To explore the impact of N-myristoylation and palmitoylation on protein targeting to chloroplasts.
  • * To determine if manipulating protein acylation can correct mislocalization and control protein destination.

Main Methods:

  • * Bioinformatics screening of chloroplast-localized protein kinases.
  • * Analysis of N-terminal protein acylation motifs, focusing on N-myristoylation.
  • * Experimental manipulation of N-myristoylation and palmitoylation sites in target proteins.

Main Results:

  • * N-terminal protein acylation, especially N-myristoylation, interferes with accurate chloroplast targeting predictions.
  • * N-myristoylation is overrepresented in the proteome but absent in known chloroplast proteins.
  • * Abolishing N-myristoylation of kinases led to nuclear accumulation, not chloroplast localization.
  • * Inhibiting N-myristoylation redirected a calcium-dependent protein kinase to chloroplasts.
  • * Artificial introduction of acylation sites suppressed chloroplast localization of other proteins.

Conclusions:

  • * N-terminal protein acylation is a critical factor in protein localization, often overlooked by predictive algorithms.
  • * Modulating N-myristoylation and palmitoylation offers a strategy to control protein targeting to chloroplasts or the nucleus.
  • * Understanding protein acylation is essential for accurate functional annotation and engineering of plant proteins.