Probing the catalytic activity and heterogeneity of Au-nanoparticles at the single-molecule level

2009 ◽  
Vol 11 (15) ◽  
pp. 2767 ◽  
Author(s):  
Weilin Xu ◽  
Jason S. Kong ◽  
Peng Chen

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Robert Alexander Wu ◽  
Yavuz S Dagdas ◽  
S Tunc Yilmaz ◽  
Ahmet Yildiz ◽  
Kathleen Collins

Telomerase synthesizes chromosome-capping telomeric repeats using an active site in telomerase reverse transcriptase (TERT) and an integral RNA subunit template. The fundamental question of whether human telomerase catalytic activity requires cooperation across two TERT subunits remains under debate. In this study, we describe new approaches of subunit labeling for single-molecule imaging, applied to determine the TERT content of complexes assembled in cells or cell extract. Surprisingly, telomerase reconstitutions yielded heterogeneous DNA-bound TERT monomer and dimer complexes in relative amounts that varied with assembly and purification method. Among the complexes, cellular holoenzyme and minimal recombinant enzyme monomeric for TERT had catalytic activity. Dimerization was suppressed by removing a TERT domain linker with atypical sequence bias, which did not inhibit cellular or minimal enzyme assembly or activity. Overall, this work defines human telomerase DNA binding and synthesis properties at single-molecule level and establishes conserved telomerase subunit architecture from single-celled organisms to humans.



2017 ◽  
Vol 19 (13) ◽  
pp. 8889-8895 ◽  
Author(s):  
Divya Singh ◽  
Srabanti Chaudhury

We present a theoretical method based on the first passage time distribution formalism to study the size-dependent catalytic activity of metal nanoparticle at the single molecule level.



2010 ◽  
Vol 132 (1) ◽  
pp. 138-146 ◽  
Author(s):  
Xiaochun Zhou ◽  
Weilin Xu ◽  
Guokun Liu ◽  
Debashis Panda ◽  
Peng Chen


2013 ◽  
pp. 102-112
Author(s):  
Memed Duman ◽  
Andreas Ebner ◽  
Christian Rankl ◽  
Jilin Tang ◽  
Lilia A. Chtcheglova ◽  
...  


Biochemistry ◽  
2021 ◽  
Vol 60 (7) ◽  
pp. 494-499
Author(s):  
Ke Lu ◽  
Cuifang Liu ◽  
Yinuo Liu ◽  
Anfeng Luo ◽  
Jun Chen ◽  
...  


Author(s):  
Jie Xu ◽  
Shuya Fan ◽  
Lei Xu ◽  
Atsushi Maruyama ◽  
Mamoru Fujitsuka ◽  
...  


2021 ◽  
Author(s):  
David A Garcia ◽  
Gregory Fettweis ◽  
Diego M Presman ◽  
Ville Paakinaho ◽  
Christopher Jarzynski ◽  
...  

Abstract Single-molecule tracking (SMT) allows the study of transcription factor (TF) dynamics in the nucleus, giving important information regarding the diffusion and binding behavior of these proteins in the nuclear environment. Dwell time distributions obtained by SMT for most TFs appear to follow bi-exponential behavior. This has been ascribed to two discrete populations of TFs—one non-specifically bound to chromatin and another specifically bound to target sites, as implied by decades of biochemical studies. However, emerging studies suggest alternate models for dwell-time distributions, indicating the existence of more than two populations of TFs (multi-exponential distribution), or even the absence of discrete states altogether (power-law distribution). Here, we present an analytical pipeline to evaluate which model best explains SMT data. We find that a broad spectrum of TFs (including glucocorticoid receptor, oestrogen receptor, FOXA1, CTCF) follow a power-law distribution of dwell-times, blurring the temporal line between non-specific and specific binding, suggesting that productive binding may involve longer binding events than previously believed. From these observations, we propose a continuum of affinities model to explain TF dynamics, that is consistent with complex interactions of TFs with multiple nuclear domains as well as binding and searching on the chromatin template.



2021 ◽  
Vol 13 (12) ◽  
pp. 14458-14469
Author(s):  
Aleksey A. Nikitin ◽  
Anton Yu Yurenya ◽  
Timofei S. Zatsepin ◽  
Ilya O. Aparin ◽  
Vladimir P. Chekhonin ◽  
...  


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