Search results for: Chengmin Qian

Items from 1 to 16 out of 16 results

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Identification of Shared and Asian‐Specific Loci for Systemic Lupus Erythematosus and Evidence for Roles of Type III Interferon Signaling and Lysosomal Function in the Disease: A Multi‐Ancestral Genome‐Wide Association Study

Yong‐Fei Wang, Wei Wei, Pattarin Tangtanatakul, Lichuan Zheng, more

Arthritis & Rheumatology > 74 > 5 > 840 - 848

Objective Systemic lupus erythematosus (SLE) is a prototypical autoimmune disease with differences in prevalence and severity among ancestral groups. This study was undertaken to identify novel genetic components, either shared by or distinct between Asian and European populations. Methods Both trans‐ancestral and ancestry‐specific meta‐analyses of genome‐wide association studies (GWAS) for SLE...

article

Non‐canonical bivalent H3K4me3K9me3 recognition by Spindlin1/C11orf84 complex

Yongming Du, Chengmin Qian

BioEssays > 44 > 4 > n/a - n/a

Bivalent chromatin with active H3K4me3 and repressive H3K27me3 was initially identified in embryonic stem cells (ESCs) to poise expression of developmental genes upon lineage commitment. Since then, many more different bivalent modifications have been demonstrated in both ESCs and fully differentiated cells. Bivalency not only spatiotemporally controls gene transcription but also acts to fine‐tune...

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Structural Insights into BAF47 and BAF155 Complex Formation

Li Yan, Si Xie, Yongming Du, Chengmin Qian

Journal of Molecular Biology > 2017 > 429 > 11 > 1650-1660

Mammalian BAF complexes are a subfamily of SWI/SNF ATP-dependent chromatin remodelers that dynamically modulate chromatin structure to regulate fundamental cellular processes including gene transcription, cell cycle control, and DNA damage response. So far, many distinct BAF complexes have been identified with polymorphic assemblies of up to 15 subunits from 29 genes. The evolutionarily conserved...

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Deposition of 5-Methylcytosine on Enhancer RNAs Enables the Coactivator Function of PGC-1α

Francesca Aguilo, SiDe Li, Natarajan Balasubramaniyan, Ana Sancho, more

Cell Reports > 2016 > 14 > 3 > 479-492

The Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1α) is a transcriptional co-activator that plays a central role in adapted metabolic responses. PGC-1α is dynamically methylated and unmethylated at the residue K779 by the methyltransferase SET7/9 and the Lysine Specific Demethylase 1A (LSD1), respectively. Interactions of methylated PGC-1α[K779me] with the Spt-Ada-Gcn5-acetyltransferase...

article

Timeless Interacts with PARP-1 to Promote Homologous Recombination Repair

Si Xie, Oliver Mortusewicz, Hoi Tang Ma, Patrick Herr, more

Molecular Cell > 2016 > 61 > 1 > 181

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Timeless Interacts with PARP-1 to Promote Homologous Recombination Repair

Si Xie, Oliver Mortusewicz, Hoi Tang Ma, Patrick Herr, more

Molecular Cell > 2015 > 60 > 1 > 163-176

Human Timeless helps stabilize replication forks during normal DNA replication and plays a critical role in activation of the S phase checkpoint and proper establishment of sister chromatid cohesion. However, it remains elusive whether Timeless is involved in the repair of damaged DNA. Here, we identify that Timeless physically interacts with PARP-1 independent of poly(ADP-ribosyl)ation. We present...

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Structure of RPA32 bound to the N‐terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins

Si Xie, Yao Lu, Jean Jakoncic, Hongzhe Sun, more

The FEBS Journal > 281 > 15 > 3382 - 3396

Replication protein A subunit RPA32 contains a C‐terminal domain that interacts with a variety of DNA damage response proteins including SMARCAL1, Tipin, UNG2 and XPA. We have solved the high‐resolution crystal structure of RPA32 C‐terminal domain (RPA32C) in complex with a 26‐amino‐acid peptide derived from the N‐terminus of SMARCAL1 (SMARCAL1N). The RPA32C–SMARCAL1N structure reveals a 1 : 1 binding...

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UHRF1 Double Tudor Domain and the Adjacent PHD Finger Act Together to Recognize K9me3-Containing Histone H3 Tail

Si Xie, Jean Jakoncic, Chengmin Qian

Journal of Molecular Biology > 2012 > 415 > 2 > 318-328

Human multi-domain-containing protein UHRF1 has recently been extensively characterized as a key epigenetic regulator for maintaining DNA methylation patterns. UHRF1 SRA domain preferentially binds to hemimethylated CpG sites, and double Tudor domain has been implicated in recognizing H3K9me3 mark, but the role of the adjacent PHD finger remains unclear. Here, we report the high-resolution crystal...

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Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase

Chengmin Qian, Xueqi Wang, Karishma Manzur, Sachchidanand, more

Journal of Molecular Biology > 2006 > 359 > 1 > 86-96

SET domain lysine methyltransferases are known to catalyze site and state-specific methylation of lysine residues in histones that is fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. Here we report the three-dimensional solution structure of the SET domain histone lysine methyltransferase (vSET) from Paramecium bursaria chlorella virus 1 bound to cofactor...

article

Structure of the Adaptor Protein p14 Reveals a Profilin-like Fold with Distinct Function

Chengmin Qian, Qiang Zhang, Xueqi Wang, Lei Zeng, more

Journal of Molecular Biology > 2005 > 347 > 2 > 309-321

The adaptor protein p14 is associated with the cytoplasmic face of late endosomes that is involved in cell-surface receptor endocytosis and it also directly interacts with MP1, a scaffolding protein that binds the MAP kinase ERK1 and its upstream kinase activator MEK1. The interaction of p14 with MP1 recruits the latter to late endosomes and the endosomal localization of p14/MP1-MEK1-ERK1 scaffolding...

article

Letter to the editor: Resonance assignments for the endosomal adaptor protein p14

Chengmin Qian, Lei Zeng, Amjad Farooq, Ming-Ming Zhou

Journal of Biomolecular NMR > 2004 > 30 > 3 > 367-368

article

Structural analysis of zinc-substituted cytochrome c

Chengmin Qian, Yong Yao, Yufeng Tong, Jinfeng Wang, more

JBIC Journal of Biological Inorganic Chemistry > 2003 > 8 > 4 > 394-400

Zinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. However, the coordination geometry of zinc in zinc-substituted cyt c has not yet been determined; two different opinions about the coordination have been reached. Here the solution structures of zinc-substituted cytochrome c that might be five-coordinated...

article

NMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: structural and magnetic characterization of azidoferricytochrome c

Yong Yao, Yibing Wu, Chengmin Qian, Keqong Ye, more

Biophysical Chemistry > 2003 > 103 > 1 > 13-23

As the exogenous ligand-cytochrome c complexes were purported to represent models for the unfolding intermediate of cytochrome c, NMR spectroscopy has been utilized to study the azide adduct of horse heart cytochrome c. The structure of azidoferricytochrome c was modeled by restrained energy minimization using paramagenetic pseudocontact shifts as constraints. The bound azide moiety was found to be...

article

Solution structure of cyanoferricytochrome c: ligand-controlled conformational flexibility and electronic structure of the heme moiety

Yong Yao, Chengmin Qian, Keqong Ye, Jinfeng Wang, more

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 4-5

Abstract. The solution structure of cyanoferricytochrome c has been determined using NMR spectroscopy. As a result of including additional constraints derived from pseudocontact shifts, a high-resolution NMR structure was obtained with high accuracy. In order to study the conformational transition between the native protein and its ligand adducts, the present structure was compared with the solution...

article

Solution structure of cyanoferricytochrome c: ligand-controlled conformational flexibility and electronic structure of the heme moiety

Yong Yao, Chengmin Qian, Keqong Ye, Jinfeng Wang, more

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 4-5 > 539-547

. The solution structure of cyanoferricytochrome c has been determined using NMR spectroscopy. As a result of including additional constraints derived from pseudocontact shifts, a high-resolution NMR structure was obtained with high accuracy. In order to study the conformational transition between the native protein and its ligand adducts, the present structure was compared with the solution structures...

article

Kinetic studies of imidazole and its methyl derivative binding to metmyoglobin: Effects of substitute methyl on the binding affinity

Chengmin Qian, Yong Yao, Yibing Wu, Wenxia Tang

BioMetals > 2000 > 13 > 3 > 267-272

The binding of imidazole and imidazole derivatives (4- and 2-MeIm) to the metMb was studied by ¹H NMR spectroscopy to elucidate the effects of different methyl substitution positions on the affinity and kinetics of binding to metMb. These exogenous ligands can form stable complexes with metMb except 2-MeIm. Kinetics and equilibrium data for the binding of imidazole and 4-MeIm to metMb have been obtained...

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