8J8Q

Structure of the four-component Paf1 complex from Saccharomyces eubayanus

Summary for 8J8Q

• Entry DOI: 10.2210/pdb8j8q/pdb
• Descriptor: CTR9-like protein, PAF1-like protein, RTF1-like protein, ... (4 entities in total)
• Functional Keywords: transcription elongation factor, the polymerase associated factor 1 (paf1) complex, transcription
• Biological source: Saccharomyces eubayanus; More
• Total number of polymer chains: 4
• Total formula weight: 136370.18

Authors

Wang, Z.,Qin, Y.,Zhou, Y.,Cao, Y. (deposition date: 2023-05-02, release date: 2023-05-24, Last modification date: 2024-11-20)

Primary citation

Qin, Y.,Zhou, Y.,Cao, Y.,Ren, Y.,Deng, P.,Jiang, J.,Wang, Z.
Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from Saccharomyces eubayanus .
Int J Mol Sci, 24:-, 2023

PubMed Abstract: The multicomponent polymerase associated factor 1 (Paf1) complex (PAF1C) is an important transcription elongation factor that upregulates RNA polymerase II-mediated genome-wide transcription. PAF1C can regulate transcription through direct association with the polymerase or by impacting the chromatin structure epigenetically. In recent years, significant progress has been made in understanding the molecular mechanisms of PAF1C. However, high-resolution structures that can clarify the interaction details among the components of the complex are still needed. In this study, we evaluated the structural core of the yeast PAF1C containing the four components Ctr9, Paf1, Cdc73 and Rtf1 at high resolution. We observed the interaction details among these components. In particular, we identified a new binding surface of Rtf1 on PAF1C and found that the C-terminal sequence of Rtf1 dramatically changed during evolution, which may account for its different binding affinities to PAF1C among species. Our work presents a precise model of PAF1C, which will facilitate our understanding of the molecular mechanism and the in vivo function of the yeast PAF1C.

PubMed: 37240075
DOI: 10.3390/ijms24108730

Experimental method

X-RAY DIFFRACTION (3.11 Å)