Ming Liu

College of Sciences

Works (3)

Updated: July 5th, 2023 14:46

2022 journal article

Densely methylated DNA traps Methyl-CpG-binding domain protein 2 but permits free diffusion by Methyl-CpG-binding domain protein 3

JOURNAL OF BIOLOGICAL CHEMISTRY, 298(10).

By: G. Leighton *, E. Irvin n, P. Kaur n, M. Liu n, C. You *, D. Bhattaram *, J. Piehler *, R. Riehn n  ...

MeSH headings : CpG Islands; DNA Methylation; DNA-Binding Proteins / metabolism; Mi-2 Nucleosome Remodeling and Deacetylase Complex / genetics; Mi-2 Nucleosome Remodeling and Deacetylase Complex / metabolism; Nucleosomes; Protein Binding; Transcription Factors / metabolism; Humans; Single Molecule Imaging
TL;DR: These studies support a model in which MBD2-NuRD strongly localizes to and compacts methylated CpG islands while MBD3-NURD can freely mobilize nucleosomes independent of methylation status. (via Semantic Scholar)
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Sources: Web Of Science, ORCID, NC State University Libraries
Added: August 29, 2022

2021 journal article

TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA

NUCLEIC ACIDS RESEARCH, 49(22), 13000–13018.

By: P. Kaur n, R. Barnes *, H. Pan n, A. Detwiler *, M. Liu n, C. Mahn n, J. Hall n , Z. Messenger n ...

MeSH headings : Animals; DNA / chemistry; DNA / genetics; DNA / metabolism; HeLa Cells; Humans; Mice, Inbred C57BL; Microscopy, Atomic Force; Nucleic Acid Conformation; Protein Binding; Shelterin Complex / genetics; Shelterin Complex / metabolism; Telomere / genetics; Telomere / metabolism; Telomere-Binding Proteins / genetics; Telomere-Binding Proteins / metabolism; Telomeric Repeat Binding Protein 2 / genetics; Telomeric Repeat Binding Protein 2 / metabolism
TL;DR: A molecular model in which TIN2 functions as an architectural protein to promote TRF2-mediated trans and cis higher-order nucleic acid structures at telomeres is proposed. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries, ORCID
Added: January 18, 2022

2020 journal article

DNA looping by two 5-methylcytosine-binding proteins quantified using nanofluidic devices

EPIGENETICS & CHROMATIN, 13(1).

By: M. Liu n, S. Movahed n, S. Dangi n, H. Pan n, P. Kaur n, S. Bilinovich *, E. Faison *, G. Leighton * ...

author keywords: DNA methylation; MeCP2; MBD2; DNA compaction
MeSH headings : 5-Methylcytosine / chemistry; 5-Methylcytosine / metabolism; Binding Sites; DNA / chemistry; DNA / metabolism; DNA Methylation; DNA-Binding Proteins / chemistry; DNA-Binding Proteins / metabolism; Epigenomics / methods; Humans; Methyl-CpG-Binding Protein 2 / chemistry; Methyl-CpG-Binding Protein 2 / metabolism; Microfluidics / instrumentation; Microfluidics / methods; Microscopy, Atomic Force / methods; Protein Binding
TL;DR: It is demonstrated that ATTO 565-labeled MBD2 is a good candidate as a staining agent for epigenetic mapping and determined that the mechanism for compaction by MeCP2 is the formation of bridges between distant DNA stretches and theformation of loops. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: April 20, 2020

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