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Biochemistry & Molecular Biology
Klaudia Adamus, Cyril Reboul, Jarrod Voss, Cheng Huang, Ralf B. Schittenhelm, Sarah N. Le, Andrew M. Ellisdon, Hans Elmlund, Marion Boudes, Dominika Elmlund
Summary: SLIK is a modified version of the SAGA complex, resulting from the C-terminal truncation of the Spt7 subunit. Both SLIK and SAGA act as coactivators in RNA polymerase II transcription, perform chromatin modifications, and exhibit similar affinity for TBP. Despite differences in subunit composition, SLIK retains similar structural features as SAGA and displays comparable DNA-binding properties.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
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Biochemistry & Molecular Biology
Prajakta Tathe, K. V. S. Rammohan Chowdary, Krushna Chandra Murmu, Punit Prasad, Subbareddy Maddika
Summary: In this study, the researchers discovered that the tyrosine phosphatase SHP-1 can dephosphorylate histone H2B and plays a critical role in transcription. SHP-1 dephosphorylates H2B at tyrosine 121, promoting H2B ubiquitination and maintaining basal autophagic flux. This study reveals the importance of SHP-1-regulated modification of H2B in eukaryotic transcription.
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Biochemistry & Molecular Biology
Michael Morgan, Tatsuya Ikenoue, Hiroaki Suga, Cynthia Wolberger
Summary: The Spt-Ada-Gcn5 acetyltransferase (SAGA) transcriptional coactivator contains a subcomplex called the deubiquitinating enzyme (DUB) module that can remove ubiquitin from histone H2B-K120. The human DUB module includes the catalytic subunit ubiquitin-specific protease 22 (USP22), which is overexpressed in certain cancers resistant to existing therapies. By screening a large library of cyclic peptides, potent inhibitors of USP22 were identified. The top hit showed high specificity for USP22 and was able to enter human cells and inhibit H2B deubiquitination.
CELL CHEMICAL BIOLOGY
(2022)
Editorial Material
Biochemistry & Molecular Biology
Seychelle M. Vos
Summary: A new study has revealed the high-resolution cryo-EM structure of the human SAGA complex, shedding light on its role in different stages of eukaryotic transcription.
NATURE STRUCTURAL & MOLECULAR BIOLOGY
(2021)
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Plant Sciences
Zuntao Xu, Enze Li, Gan Xue, Cheng Zhang, Yachun Yang, Yong Ding
Summary: This study reveals that OsHUB2 represses the function of OsTrx1 and H3K4me3 levels at Ehd1, and suggests that OsHUB2-mediated H2B ubiquitination plays critical roles together with H3K4me3 in rice heading date regulation.
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Biochemistry & Molecular Biology
Patrick A. Grant, Fred Winston, Shelley L. Berger
Summary: This article reviews early genetic and biochemical experiments that led to the discovery of SAGA complex and the elucidation of its multiple activities in regulating gene transcription in eukaryotes.
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
(2021)
Article
Cell Biology
Shinya Takahata, Saori Chida, Aoi Ohnuma, Motoyoshi Ando, Takahiro Asanuma, Yota Murakami
Summary: In heterochromatin, Spt16 recruitment is mediated by Pob3 and HP1/Swi6. Pob3 recruits Spt16 through its Spt16 dimerization and PH domains, while HP1/Swi6 recruits Spt16 through physical interaction of the Swi6 CSD and Spt16 peptidase-like domains.
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Biochemistry & Molecular Biology
Zhiheng Deng, Huasong Ai, Maoshen Sun, Zebin Tong, Yunxiang Du, Qian Qu, Liying Zhang, Ziyu Xu, Shixian Tao, Qiang Shi, Jia-Bin Li, Man Pan, Lei Liu
Summary: This study elucidates the mechanism of H2B monoubiquitylation and highlights the critical role of nucleosomal DNA in mediating E3 ligase recognition.
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Cell Biology
Liying Wang, Zhiliang Xu, Libin Wang, Chao Liu, Huafang Wei, Ruidan Zhang, Yinghong Chen, Lina Wang, Wenwen Liu, Sai Xiao, Wei Li, Wei Li
Summary: The study reveals that RNF20 is crucial for early stage somatic cell reprogramming, with Rnf20 knockout leading to failure in reprogramming at the initial stage. The absence of RNF20 affects the transcription of MET-related genes and early pluripotency genes, ultimately hindering the establishment of a pluripotent gene network.
CELL PROLIFERATION
(2021)
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Oncology
Lucile M. Jeusset, Kirk J. McManus
Summary: Monoubiquitination of histone H2B on lysine 120 plays a crucial role in various biological processes. Aberrant regulation of H2Bub1 can lead to transcriptional reprogramming and genome instability, thereby promoting oncogenesis. Understanding the misregulation of H2Bub1 may reveal novel drug targets and therapeutic strategies for cancer treatment.
SEMINARS IN CANCER BIOLOGY
(2022)
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Biochemistry & Molecular Biology
Fengling Lai, Yibin Cheng, Juan Zou, Haoyu Wang, Wang Zhu, Xin Wang, Hanhua Cheng, Rongjia Zhou
Summary: This study examined histone modifications in gonadal differentiation, identifying new modification sites and their relationship with different types of gonadal differentiation. The research also discovered a testis-enriched histone modification site associated with spermatogenesis, emphasizing the importance of histone modifications in the transcriptional regulation of sex-determining genes during gonadal development.
INTERNATIONAL JOURNAL OF BIOLOGICAL SCIENCES
(2021)
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Biochemistry & Molecular Biology
Manjit Kumar Srivastav, Neha Agarwal, Poonam Poonia, Krishnamurthy Natarajan
Summary: This study elucidates how transcriptional regulators in Candida albicans control gene expression levels under iron deprivation conditions, thereby affecting iron homeostasis. The trimeric HAP complex promotes transcription of certain genes and regulates expression levels through histone modifications to maintain cellular iron balance.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Article
Multidisciplinary Sciences
Tasniem Fetian, Brendan M. McShane, Nicole L. Horan, Donya N. Shodja, Jason D. True, Amber L. Mosley, Karen M. Arndt
Summary: Histone modifications coupled to transcription elongation play important roles in regulating gene expression. The Paf1 transcription elongation complex (Paf1C) interacts with the ubiquitin conjugase Rad6 through its histone modification domain (HMD), leading to H2BK123 ubiquitylation. The specific interface between a transcription elongation factor and a ubiquitin conjugase guides substrate selection during active gene expression.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2023)
Article
Cell Biology
Meagan Jezek, Winny Sun, Maraki Y. Negesse, Zachary M. Smith, Alexander Orosz, Erin M. Green
Summary: Set1 is an H3K4 methyltransferase involved in various genomic functions. It plays a role in subtelomeric gene repression through its catalytic activity towards H3K4 and regulates telomere length through its catalytic activity but likely independent of the H3K4 substrate. Set1 also calibrates the abundance of critical telomere maintenance proteins through transcriptional and posttranscriptional pathways. These findings provide new insights into the roles of Set1 in telomere maintenance and have implications for Set1-related methyltransferases in other systems.
MOLECULAR BIOLOGY OF THE CELL
(2023)
Article
Biochemistry & Molecular Biology
Sara T. Haile, Sanim Rahman, James K. Fields, Benjamin C. Orsburn, Namandje N. Bumpus, Cynthia Wolberger
Summary: The SAGA complex, which includes the HAT module, is a transcriptional co-activator that modifies histones through acetylation and deubiquitination. The SWIRM domain plays a crucial role in incorporating the HAT module into the SAGA complex. Deletion of the SWIRM domain results in loss of the HAT module and decreases the deubiquitinating activity of SAGA.
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
(2023)