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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Structural insights into Paf1 complex assembly and histone binding.

Xinlei Chu1, Xiaohong Qin, Huisha Xu

  • 1State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China, College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China and Synergetic Innovation Center of Chemical Science and Engineering, 94 Weijin Road, Tianjin 300071, China.

Nucleic Acids Research
|September 17, 2013
PubMed
Summary

The Paf1/Leo1 subcomplex forms a stable heterodimer crucial for the Paf1 complex (PAF1C) assembly and function. This complex binds to histone proteins, impacting transcription and histone modifications.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Epigenetics

Background:

  • The Paf1 complex (PAF1C) is essential for RNA polymerase II transcription elongation and histone modification.
  • PAF1C is involved in various cellular processes including embryonic development and stem cell maintenance.

Purpose of the Study:

  • To determine the structure of the human Paf1/Leo1 subcomplex within PAF1C.
  • To elucidate the assembly mechanism of PAF1C and its substrate recognition.

Main Methods:

  • X-ray crystallography to determine the structure of the Paf1/Leo1 heterodimer.
  • Biochemical assays to investigate subunit interactions and binding to histones.

Main Results:

  • The Paf1 and Leo1 subunits form a tightly associated heterodimer via antiparallel beta-sheet interactions.
  • Leo1 binds to PAF1C through Paf1, with Ctr9 acting as the central scaffold protein.
  • The Paf1/Leo1 heterodimer is essential for binding to histone H3, the histone octamer, and nucleosomes.

Conclusions:

  • The structure of the Paf1/Leo1 heterodimer provides insights into PAF1C assembly.
  • Understanding PAF1C assembly and histone binding is key to comprehending PAF1C-regulated histone modifications.