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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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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...
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Updated: Dec 5, 2025

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Decrypting UFMylation: How Proteins Are Modified with UFM1.

Sayanika Banerjee1, Manoj Kumar1, Reuven Wiener1

  • 1Department of Biochemistry and Molecular Biology, The Institute for Medical Research Israel-Canada, Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel.

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|October 17, 2020
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Ubiquitin-like modifier 1 (UFM1) is a poorly understood protein modifier. This review compiles current data on UFM1 (UFMylation) and suggests its physiological significance is underestimated.

Keywords:
UBA5UFC1UFL1UFM1UFMylationconjugating enzymesubiquitin-like proteins

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Humans utilize ubiquitin (Ub) and ubiquitin-like proteins (UBLs) for protein modification.
  • Ubiquitin-fold modifier 1 (UFM1) is a UBL with limited current understanding.
  • UFMylation, the modification by UFM1, is incompletely characterized.

Purpose of the Study:

  • To review existing data on UFM1.
  • To consolidate knowledge from structural biology, biochemistry, and cell biology.
  • To highlight the potential underestimation of UFM1's physiological roles.

Main Methods:

  • Literature review of UFM1 research.
  • Analysis of data from structural biology studies.
  • Synthesis of findings from biochemical and cell biology experiments.

Main Results:

  • Current understanding of UFMylation is fragmented.
  • Data integration reveals gaps in knowledge.
  • UFM1 modification pathways require further elucidation.

Conclusions:

  • The physiological importance of UFM1 modification is likely underestimated.
  • Further research is needed to fully understand UFMylation.
  • UFM1 represents a significant area for future biological investigation.