Preston James Countryman

Works (7)

Updated: July 6th, 2023 16:20

2020 journal article

Single-molecule level structural dynamics of DNA unwinding by human mitochondrial Twinkle helicase

JOURNAL OF BIOLOGICAL CHEMISTRY, 295(17), 5564–5576.

By: P. Kaur n, M. Longley *, H. Pan n, W. Wang  n, P. Countryman n, H. Wang n , W. Copeland *

author keywords: atomic force microscopy (AFM); DNA binding protein; DNA helicase; DNA replication; mitochondrial disease; mitochondrial DNA (mtDNA); single-molecule biophysics; ssDNA-binding protein (SSB); structural dynamics; Twinkle helicase
MeSH headings : DNA / analysis; DNA / metabolism; DNA Helicases / analysis; DNA Helicases / metabolism; Humans; Microscopy, Atomic Force; Mitochondria / metabolism; Mitochondrial Proteins / analysis; Mitochondrial Proteins / metabolism; Nucleic Acid Conformation; Protein Binding; Protein Multimerization; Recombinant Proteins / analysis; Recombinant Proteins / metabolism
TL;DR: Atomic force microscopy imaging in air and liquids is employed to visualize ring assembly, DNA binding, and unwinding activity of individual Twinkle hexamers at the single-molecule level and finds that the addition of mitochondrial single-stranded DNA–binding protein both influences the ways Twinkle loads onto defined DNA substrates and stabilizes the unwound ssDNA product. (via Semantic Scholar)
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Source: Web Of Science
Added: May 18, 2020

2016 journal article

Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2

Scientific Reports, 6.

By: P. Kaur, D. Wu, J. Lin, P. Countryman, K. Bradford, D. Erie, R. Riehn , P. Opresko, H. Wang 

Source: NC State University Libraries
Added: August 6, 2018

2016 journal article

Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairing

NUCLEIC ACIDS RESEARCH, 44(13), 6363–6376.

By: J. Lin n, P. Countryman n, H. Chen *, H. Pan n, Y. Fan*, Y. Jiang *, P. Kaur n, W. Miao * ...

MeSH headings : AT-Hook Motifs / genetics; Chromatids / genetics; Chromatids / ultrastructure; Chromosome Segregation / genetics; DNA-Binding Proteins / genetics; Humans; Microscopy, Atomic Force; Mitosis / genetics; Nuclear Proteins / genetics; Nuclear Proteins / metabolism; Telomere / genetics; Telomere / ultrastructure; Telomere-Binding Proteins / genetics; Telomere-Binding Proteins / metabolism; Telomeric Repeat Binding Protein 1 / genetics; Telomeric Repeat Binding Protein 1 / metabolism
TL;DR: The results suggest that at telomeres cohesion relies on the molecular interplay between TRF1 and SA1 to promote DNA–DNA pairing, while along chromosomal arms the core cohesin assembly might also depend on SA1 1D diffusion on DNA and sequence-specific DNA binding. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2014 journal article

Probing transient protein-mediated DNA linkages using nanoconfinement

Biomicrofluidics, 8(3).

By: M. Roushan, P. Kaur, A. Karpusenko, P. Countryman, C. Ortiz, S. Lim , H. Wang , R. Riehn 

Source: NC State University Libraries
Added: August 6, 2018

2014 conference paper

Single-molecule imaging reveals DNA-binding properties of cohesin proteins SA1 and SA2.

Environmental and Molecular Mutagenesis, 55, S29–29.

By: J. Lin, P. Kaur, H. Chen, P. Countryman, M. Roushan, D. Flaherty, E. Brennan, C. You ...

Source: NC State University Libraries
Added: August 6, 2018

2014 journal article

TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres

NUCLEIC ACIDS RESEARCH, 42(4), 2493–2504.

By: J. Lin n, P. Countryman n, N. Buncher  n, P. Kaur n, E. Longjiang n, Y. Zhang n, G. Gibson  n, C. You  n ...

MeSH headings : DNA / chemistry; DNA / metabolism; Diffusion; Protein Binding; Protein Structure, Tertiary; Repetitive Sequences, Nucleic Acid; Telomere / chemistry; Telomere / metabolism; Telomeric Repeat Binding Protein 1 / metabolism; Telomeric Repeat Binding Protein 2 / chemistry; Telomeric Repeat Binding Protein 2 / metabolism
TL;DR: It is proposed that the TRF proteins use 1D sliding to find protein partners and assemble the shelterin complex, which in turn stabilizes the interaction with specific telomeric DNA. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2014 journal article

Unraveling secrets of telomeres: One molecule at a time

DNA REPAIR, 20, 142–153.

By: J. Lin n, P. Kaur n, P. Countryman n, P. Opresko * & H. Wang n 

author keywords: Telomeres; Single-molecule imaging; Atomic force microscopy; Fluorescence microscopy; FRET; Laser tweezers; Magnetic tweezers; Protein DNA interactions
MeSH headings : Animals; Fluorescence Resonance Energy Transfer / methods; Humans; Microscopy, Atomic Force / methods; Microscopy, Fluorescence / methods; Optical Tweezers; Telomere / chemistry; Telomere / metabolism; Telomere-Binding Proteins / chemistry; Telomere-Binding Proteins / metabolism
TL;DR: This review presents a brief overview of the principles of single-molecule imaging and manipulation techniques and highlights results obtained from applying these single- molecule techniques for studying structure, dynamics and functions of G-quadruplexes, telomerase, and shelterin proteins. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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