Publications by authors named "Suman Wang"

NSUN6 preferentially catalyzes the methylation of cytosine nucleotides in mRNA substrates, which enhances transcription. Dysregulation of NSUN6 catalysis drives the oncogenesis of certain cancers. In this study, we determined the crystal structure of human NSUN6 in complex with its S-adenosyl-L-methionine analog and a bound NECT-2 3'-UTR RNA substrate at 2.

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Article Synopsis
  • The pairing center (PC) in C. elegans chromosomes is vital for homolog pairing and synapsis, with specific DNA motifs that recruit certain meiosis proteins (ZIM-1, ZIM-2, ZIM-3, HIM-8).
  • Researchers have determined the crystal structures of the DNA binding domains of HIM-8, ZIM-1, and ZIM-2 bound to their respective PC DNA motifs, revealing important details about how they interact.
  • The study highlights that specific DNA-contacting residues are concentrated in the ZF1-2 domains and that the CTD may enhance the flexibility and specificity of binding to different PC DNA motifs, indicating a co-evolution of these elements.
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The class-II transactivator (CIITA) is the master regulator of MHC class-II gene expression and hence the adaptive immune response. Three cell type-specific promoters (pI, pIII, and pIV) are involved in the regulation of CIITA expression, which can be induced by IFN-γ in non-immune cells. While key regulatory elements have been identified within these promoters, our understanding of the transcription factors regulating CIITA expression is incomplete.

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Multiple proteins bind to telomeric DNA and are important for the role of telomeres in genome stability. A recent study established a broad-complex, tramtrack and bric-à-brac - zinc finger (BTB-ZF) protein, ZBTB10 (zinc finger and BTB domain-containing protein 10), as a telomeric variant repeat-binding protein at telomeres that use an alternative method for lengthening telomeres). ZBTB10 specifically interacts with the double-stranded telomeric variant repeat sequence TTGGGG by employing its tandem C2H2 zinc fingers (ZF1-2).

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The RNA recognition motif (RRM) binds to nucleic acids as well as proteins. More than one such domain is found in the pre-mRNA processing hnRNP proteins. While the mode of RNA recognition by RRMs is known, the molecular basis of their protein interaction remains obscure.

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The microprocessor complex cleaves the primary transcript of microRNA (pri-miRNA) to initiate miRNA maturation. Microprocessor is known to consist of RNase III DROSHA and dsRNA-binding DGCR8. Here, we identify Enhancer of Rudimentary Homolog (ERH) as a new component of Microprocessor.

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Telomeres are nucleoprotein structures at the ends of linear chromosomes and present an essential feature for genome integrity. Vertebrate telomeres usually consist of hexameric TTAGGG repeats, however, in cells that use the alternative lengthening of telomeres (ALT) mechanism, variant repeat sequences are interspersed throughout telomeres. Previously, it was shown that NR2C/F transcription factors bind to TCAGGG variant repeats and contribute to telomere maintenance in ALT cells.

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Biosensors are analytical devices, which use biological interactions to provide either qualitative or quantitative results. They are extensively employed in many fields such as clinical diagnosis and biomedicine, military applications, anti-terrorism, farm, garden and veterinary analysis, process control, fermentation control and analysis, pharmaceutical and drug analysis, food and drink production and analysis, pollution control and monitoring, microbiology, bacterial and viral analysis, mining, and industrial and toxic gases. The biosensor market has significantly increased and will be mushrooming in the next decade.

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