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Related Concept Videos

Covalently Linked Protein Regulators02:04

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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 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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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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Histone Modification02:32

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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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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Related Experiment Video

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

Michael J Matunis1, Manuel S Rodriguez2

  • 1Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, 615 North Wolfe St., Room W8118, Baltimore, MD, 21205, USA. mmatunis@jhsph.edu.

Methods in Molecular Biology (Clifton, N.J.)
|September 16, 2016
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Summary

Small ubiquitin-related modifier (SUMO)ylation, a key protein modification, impacts diverse cellular processes. New methodologies are emerging to study this complex, reversible system and its regulatory enzymes.

Keywords:
HistoryMethodologiesSUMOylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Small ubiquitin-related modifier (SUMO)ylation, initially identified in the mid-1990s, has evolved from a nuclear-focused modification to a broadly recognized cellular regulator.
  • Early research concentrated on SUMOylation's roles in transcription, chromatin structure, and DNA repair within the nucleus.

Observation:

  • SUMOylation is now understood to influence a wide array of cellular processes in both the nucleus and cytoplasm.
  • The dynamic regulation of SUMOylation involves specific conjugating enzymes and proteases, highlighting its complex nature.
  • Recent discoveries include ubiquitin-SUMO hybrid chains and SUMO-interacting motifs, indicating intricate regulatory mechanisms.

Findings:

  • SUMOylation's functional scope extends beyond its initially recognized nuclear roles.
  • The system is characterized by dynamic reversibility, actively controlled by enzymatic machinery.
  • Complex interactions, such as hybrid chains and multi-protein complexes, are integral to SUMOylation's function.

Implications:

  • Understanding SUMOylation is crucial for deciphering fundamental cellular mechanisms.
  • New methodologies are being developed to investigate SUMOylation events in vitro and in vivo.
  • This research opens avenues for exploring novel therapeutic targets and understanding disease pathogenesis.