Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>

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 chromati...

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Main Authors: Yan Qin, Yuqiao Zhou, Yinghua Cao, Yanpeng Ren, Pujuan Deng, Junyi Jiang, Zhanxin Wang
Format: Article
Language:English
Published: MDPI AG 2023-05-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/24/10/8730
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author Yan Qin
Yuqiao Zhou
Yinghua Cao
Yanpeng Ren
Pujuan Deng
Junyi Jiang
Zhanxin Wang
author_facet Yan Qin
Yuqiao Zhou
Yinghua Cao
Yanpeng Ren
Pujuan Deng
Junyi Jiang
Zhanxin Wang
author_sort Yan Qin
collection DOAJ
description 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.
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spelling doaj.art-164829b03244487cabaacd8e853202692023-11-18T01:40:50ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-05-012410873010.3390/ijms24108730Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>Yan Qin0Yuqiao Zhou1Yinghua Cao2Yanpeng Ren3Pujuan Deng4Junyi Jiang5Zhanxin Wang6Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, 19 Xinjiekouwai Avenue, Beijing 100875, ChinaThe 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.https://www.mdpi.com/1422-0067/24/10/8730Paf1 complexRtf1transcription elongationevolutioncrystal structure
spellingShingle Yan Qin
Yuqiao Zhou
Yinghua Cao
Yanpeng Ren
Pujuan Deng
Junyi Jiang
Zhanxin Wang
Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>
International Journal of Molecular Sciences
Paf1 complex
Rtf1
transcription elongation
evolution
crystal structure
title Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>
title_full Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>
title_fullStr Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>
title_full_unstemmed Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>
title_short Structural Basis of the Transcriptional Elongation Factor Paf1 Core Complex from <i>Saccharomyces eubayanus</i>
title_sort structural basis of the transcriptional elongation factor paf1 core complex from i saccharomyces eubayanus i
topic Paf1 complex
Rtf1
transcription elongation
evolution
crystal structure
url https://www.mdpi.com/1422-0067/24/10/8730
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