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Related Concept Videos

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.
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.
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the addition of a...

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Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
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Modulating protein-DNA interactions by post-translational modifications at disordered regions.

Dana Vuzman1, Yonit Hoffman, Yaakov Levy

  • 1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. dana.golbin@weizmann.ac.il

Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
|December 17, 2011
PubMed
Summary

Post-translational modifications like phosphorylation and acetylation commonly occur on disordered tails of DNA-binding proteins. These modifications can alter DNA binding affinity by changing the protein

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Intrinsically disordered regions (IDRs), especially disordered tails, are prevalent in DNA-binding proteins (DBPs).
  • The function of these disordered tails in modulating DNA interactions is influenced by their charged residue composition and distribution.
  • Post-translational modifications (PTMs) like phosphorylation and acetylation can alter the properties of disordered tails, potentially affecting DNA binding.

Purpose of the Study:

  • To analyze the prevalence and distribution of acetylation and phosphorylation sites on disordered tails of human DBPs.
  • To investigate potential differences in PTM patterns between DBPs and non-DBPs.
  • To understand how PTMs on disordered tails modulate protein-DNA interactions.

Main Methods:

  • Analysis of large human protein datasets (3398 for acetylation, 8943 for phosphorylation).
  • Identification and quantification of acetylation and phosphorylation sites within disordered regions, specifically disordered tails.
  • Comparison of PTM site distribution in DBPs versus non-DBPs.

Main Results:

  • Both acetylation and phosphorylation are common on disordered tails of DBPs, with specific site densities reported.
  • Phosphorylation sites are abundant in disordered regions of both DBPs and non-DBPs.
  • Acetylation sites are frequent in disordered tails of DBPs but often found in ordered regions of non-DBPs, suggesting distinct roles.

Conclusions:

  • PTMs on disordered tails of DBPs can significantly modulate protein-DNA interactions by altering tail properties.
  • The extent of modulation is dependent on the number and interplay (cross-talk) of PTMs.
  • Acetylation may have different functional implications in DBPs compared to non-DBPs due to its localization patterns.