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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Conservation of Protein Domains Over Different Proteins02:26

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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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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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Phosphoinositides and PIPs01:42

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Structural basis for evolutionarily conserved interactions between TFIIS and Paf1C.

Jie Gao1, Miki Jishage2, Yuzhu Wang3

  • 1MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China; Department of Ophthalmology, The Second Affiliated Hospital of Anhui Medical University, 678 Furong Road, Hefei, Anhui, PR China.

International Journal of Biological Macromolecules
|September 11, 2023
PubMed
Summary
This summary is machine-generated.

Transcription factor TFIIS binds Leo1 within the Paf1C complex, crucial for RNA polymerase II transcription. Structural studies reveal species-specific interactions, highlighting evolutionary variations in transcription regulation.

Keywords:
LW domainLeo1Paf1C complexProtein structureTFIISTranscription regulation

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Evolutionary Biology

Background:

  • The transcription elongation factor TFIIS interacts with the Paf1 complex (Paf1C) to promote processive transcription by RNA polymerase II (Pol II).
  • Understanding the structural basis of TFIIS-Paf1C interaction is key to elucidating transcription regulation mechanisms.

Purpose of the Study:

  • To determine the crystal structure of the TFIIS LW domain in complex with the Leo1 LFG motif from Trypanosoma.
  • To elucidate the structural basis of TFIIS-Paf1C interactions and their species-specific variations.

Main Methods:

  • X-ray crystallography was used to determine the structures of TFIIS LW domains (apo and complexed forms) from Trypanosoma, yeast, and human.
  • Structural analysis focused on conserved hydrophobic cores and conformational changes in the TFIIS LW domain upon Leo1 binding.

Main Results:

  • Conserved hydrophobic cores mediate TFIIS LW domain interactions with Leo1 across species.
  • Trypanosoma Leo1 binding induces a unique conformational change in the TFIIS LW domain's α6 helix, absent in yeast and human.
  • This conformational difference accounts for higher binding affinity in Trypanosoma and indicates species-specific interaction variations.

Conclusions:

  • The TFIIS LW domain interaction with Leo1's LFG motif is essential for anchoring the Paf1C complex.
  • These findings provide a detailed structural basis for TFIIS-Paf1C interaction and shed light on the evolution of transcription regulation by these factors.