Zobrazeno 1 - 10
of 228
pro vyhledávání: '"Timothy M. Lohman"'
Autor:
Sean P. Carney, Wen Ma, Kevin D. Whitley, Haifeng Jia, Timothy M. Lohman, Zaida Luthey-Schulten, Yann R. Chemla
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
UvrD is a model helicase from the non-hexameric Superfamily 1. Here, the authors use optical tweezers to measure directly the stepwise translocation of UvrD along a DNA hairpin, and propose a mechanism in which UvrD moves one base pair at a time, but
Externí odkaz:
https://doaj.org/article/787da31e7c364e8b9f5fc0478dc6983b
Autor:
Britney Johnson, Patrick McConnell, Alex G. Kozlov, Marlene Mekel, Timothy M. Lohman, Michael L. Gross, Gaya K. Amarasinghe, John A. Cooper
Publikováno v:
Cell Reports, Vol 23, Iss 9, Pp 2795-2804 (2018)
Actin assembly is important for cell motility. The ability of actin subunits to join or leave filaments via the barbed end is critical to actin dynamics. Capping protein (CP) binds to barbed ends to prevent subunit gain and loss and is regulated by p
Externí odkaz:
https://doaj.org/article/f8380583d0ab4e5ea1829184075c0d34
Publikováno v:
Nucleic Acids Research. 51:2284-2297
Escherichia coli single stranded (ss) DNA binding protein (SSB) plays essential roles in DNA maintenance. It binds ssDNA with high affinity through its N-terminal DNA binding core and recruits at least 17 different SSB interacting proteins (SIPs) tha
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Replication protein A (RPA) is a eukaryotic single-stranded (ss) DNA-binding (SSB) protein that is essential for all aspects of genome maintenance. RPA binds ssDNA with high affinity but can also diffuse along ssDNA. By itself, RPA is capable of tran
Autor:
Haifeng Jia, Yann R. Chemla, Sean P. Carney, Zaida Luthey-Schulten, Timothy M. Lohman, Wen Ma, Kevin D. Whitley
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications
Nature Communications
UvrD, a model for non-hexameric Superfamily 1 helicases, utilizes ATP hydrolysis to translocate stepwise along single-stranded DNA and unwind the duplex. Previous estimates of its step size have been indirect, and a consensus on its stepping mechanis
Publikováno v:
Biophysical Journal. 122:63a-64a
Publikováno v:
Nucleic Acids Research
Escherichia coli RecO is a recombination mediator protein that functions in the RecF pathway of homologous recombination, in concert with RecR, and interacts with E. coli single stranded (ss) DNA binding (SSB) protein via the last 9 amino acids of th
Autor:
Steven J. Sandler, Antoine M. van Oijen, Nicholas E. Dixon, Lisanne M. Spenkelink, James L. Keck, Alexander G. Kozlov, Michael M. Cox, Elizabeth A. Wood, Timothy M. Lohman, Katarzyna Dubiel, Slobodan Jergic, Camille Henry
Publikováno v:
Nucleic Acids Research
Bacterial single-stranded DNA-binding proteins (SSBs) bind single-stranded DNA and help to recruit heterologous proteins to their sites of action. SSBs perform these essential functions through a modular structural architecture: the N-terminal domain
Autor:
Ankita Chadda, Drake Jensen, Eric J. Tomko, Ana Ruiz Manzano, Binh Nguyen, Timothy M. Lohman, Eric A. Galburt
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Significance Mycobacterium tuberculosis ( Mtb ) is an intracellular pathogen that causes tuberculosis and is exposed to oxidative insults from immune system macrophages. Mtb UvrD1 plays a role in DNA repair during infection and has been suggested to
Autor:
Alexander G. Kozlov, Xian Cheng, Hongshan Zhang, Min Kyung Shinn, Elizabeth Weiland, Binh Nguyen, Irina A. Shkel, Emily Zytkiewicz, Ilya J. Finkelstein, M. Thomas Record, Timothy M. Lohman
Publikováno v:
J Mol Biol
E. coli single-stranded-DNA binding protein (EcSSB) displays nearest-neighbor (NN) and non-nearest-neighbor (NNN)) cooperativity in binding ssDNA during genome maintenance. NNN cooperativity requires the intrinsically-disordered linkers (IDL) of the