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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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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...
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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DSS1/Sem1, a Multifunctional and Intrinsically Disordered Protein.

Birthe B Kragelund1, Signe M Schenstrøm1, Caio A Rebula1

  • 1Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.

Trends in Biochemical Sciences
|March 6, 2016
PubMed
Summary

DSS1/Sem1 is a disordered protein crucial for proteasome function and other cellular processes. It acts as a versatile adhesive, preventing unwanted interactions during protein complex assembly.

Keywords:
DNA repairPCI domainintrinsically disordered proteinsmRNA exportproteasomeprotein degradation

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Area of Science:

  • Molecular Biology
  • Protein Biochemistry

Background:

  • DSS1/Sem1 is an intrinsically disordered protein with diverse cellular roles.
  • It functions as a subunit of the 26S proteasome and interacts with multiple other protein complexes.

Purpose of the Study:

  • To summarize the structural and functional aspects of DSS1/Sem1.
  • To emphasize its multifunctional and disordered properties.

Main Methods:

  • Literature review and synthesis of existing structural and functional data on DSS1/Sem1.

Main Results:

  • DSS1/Sem1 is involved in homologous recombination, RNA splicing, transcription, and mRNA nuclear export.
  • As a proteasome subunit, it aids in assembly and may act as a ubiquitin receptor.
  • The protein's disordered nature allows it to adopt different structures for diverse interactions.

Conclusions:

  • DSS1/Sem1 functions as a polyanionic adhesive, preventing nonproductive interactions in protein assembly.
  • Its unique structural adaptability enables association with various multisubunit complexes.