Výsledky vyhledávání - "Charles E Bell"

Akademický článek

Half a century after their discovery: Structural insights into exonuclease and annealase proteins catalyzing recombineering

Autor: Lucy J. Fitschen, Timothy P. Newing, Nikolas P. Johnston, Charles E. Bell, Gökhan Tolun

Publikováno v: Engineering Microbiology, Vol 4, Iss 1, Pp 100120- (2024)

Recombineering is an essential tool for molecular biologists, allowing for the facile and efficient manipulation of bacterial genomes directly in cells without the need for costly and laborious in vitro manipulations involving restriction enzymes. Th

Externí odkaz: https://doaj.org/article/26db5ad3b59847bd925a78c8f3e21d7a

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Akademický článek

Structure of a RecT/Redβ family recombinase in complex with a duplex intermediate of DNA annealing

Autor: Brian J. Caldwell, Andrew S. Norris, Caroline F. Karbowski, Alyssa M. Wiegand, Vicki H. Wysocki, Charles E. Bell

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)

Specific ssDNA binding proteins promote the annealing of complementary strands. Here the authors reveal an intermediate of annealing in which a duplex DNA is bound in an unusual conformation that is highly extended and unwound for the ssDNA binding p

Externí odkaz: https://doaj.org/article/aac4a04f2d004c9b9656c68c765f8d2d

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Structure of a Rad52 homolog from bacteriophage in complex with a novel duplex intermediate of DNA annealing

Autor: Brian J. Caldwell, Andrew Norris, Vicki H. Wysocki, Charles E. Bell

Human Rad52 protein binds to ssDNA and promotes the annealing of complementary strands. This activity is central to multiple DNA repair pathways and Rad52 is a target for cancer therapeutics. Previous crystal structures of the DNA binding domain of R

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ef3b878f1524a46aad9b59e4880f97b7
https://doi.org/10.1101/2022.03.17.484533

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Mycobacterium tuberculosis encodes a YhhN family membrane protein with lysoplasmalogenase activity that protects against toxic host lysolipids

Autor: Marianne S. Jurkowitz, Abul K. Azad, Paula C. Monsma, Tracy L. Keiser, Jean Kanyo, TuKiet T. Lam, Charles E. Bell, Larry S. Schlesinger

Publikováno v: The Journal of biological chemistry. 298(5)

The pathogen Mycobacterium tuberculosis (M.tb) resides in human macrophages, wherein it exploits host lipids for survival. However, little is known about the interaction between M.tb and macrophage plasmalogens, a subclass of glycerophospholipids wit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb70cc8ac0e435df89b244c876e32d2a
https://pubmed.ncbi.nlm.nih.gov/35314194

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Mutational Analysis of Redβ Single Strand Annealing Protein: Roles of the 14 Lysine Residues in DNA Binding and Recombination In Vivo

Autor: Carter T. Wheat, Brian J. Caldwell, Shalya Ta, Katerina Zakharova, Charles E. Bell

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 14
International Journal of Molecular Sciences, Vol 22, Iss 7758, p 7758 (2021)

Redβ is a 261 amino acid protein from bacteriophage λ that promotes a single-strand annealing (SSA) reaction for repair of double-stranded DNA (dsDNA) breaks. While there is currently no high-resolution structure available for Redβ, models of its

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::543fda6f69d1060e4ca9714ded99b932

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Crystal structure of the Redβ C-terminal domain in complex with λ Exonuclease reveals an unexpected homology with λ Orf and an interaction withEscherichia colisingle stranded DNA binding protein

Autor: Brian J Caldwell, Ekaterina Zakharova, Gabriel T Filsinger, Timothy M Wannier, Jordan P Hempfling, Lee Chun-Der, Dehua Pei, George M Church, Charles E Bell

Publikováno v: Nucleic Acids Research

Bacteriophage λ encodes a DNA recombination system that includes a 5′-3′ exonuclease (λ Exo) and a single strand annealing protein (Redβ). The two proteins form a complex that is thought to mediate loading of Redβ directly onto the single-str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b505df61636887a5e808551950ae7c2
https://doi.org/10.1093/nar/gky1309

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Oligomeric complexes formed by Redβ single strand annealing protein in its different DNA bound states

Autor: Charles E. Bell, Carter T. Wheat, Vicki H. Wysocki, Deepanshu Choudhary, Marcos Sotomayor, Ekaterina Zakharova, Brian J. Caldwell, Andrew Norris, Christopher E. Smith

Publikováno v: Nucleic Acids Research

Redβ is a single strand annealing protein from bacteriophage λ that binds loosely to ssDNA, not at all to pre-formed dsDNA, but tightly to a duplex intermediate of annealing. As viewed by electron microscopy, Redβ forms oligomeric rings on ssDNA s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7557f684c2639ea606e41f61e6fec3ee
https://pubmed.ncbi.nlm.nih.gov/33693865

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Integrated Use of Biochemical, Native Mass Spectrometry, Computational, and Genome-Editing Methods to Elucidate the Mechanism of a Salmonella deglycase

Autor: Charles E. Bell, Brian M. M. Ahmer, Nicholas Thomsen, Anice Sabag-Daigle, Steffen Lindert, Venkat Gopalan, Tien-Hao Chen, Anindita Sengupta, Jikang Wu, Vicki H. Wysocki, Justin T Seffernick, Angela Di Capua

Publikováno v: J Mol Biol

Salmonellais a foodborne pathogen that causes annually millions of cases of salmonellosis globally, yet Salmonella-specific antibacterials are not available. During inflammation, Salmonella utilizes the Amadori compound fructose-asparagine (F-Asn) as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::553c67dcc32b6b9d158d8d24dfde2ab9
https://pubmed.ncbi.nlm.nih.gov/31493410

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