Zobrazeno 1 - 10
of 207
pro vyhledávání: '"Reid C Johnson"'
Autor:
Wenyang Chen, Sridhar Mandali, Stephen P Hancock, Pramod Kumar, Michael Collazo, Duilio Cascio, Reid C Johnson
Publikováno v:
eLife, Vol 7 (2018)
IS607-family transposons are unusual because they do not have terminal inverted repeats or generate target site duplications. They encode two protein-coding genes, but only tnpA is required for transposition. Our X-ray structures confirm that TnpA is
Externí odkaz:
https://doaj.org/article/ffeffce569774af6adcaf2932fc06da3
Autor:
Yuji Itoh, Sridhar Mandali, Cheng Tan, Reid C. Johnson, Yining Wu, Shoji Takada, Eriko Mano, Kiyoto Kamagata
Publikováno v:
Nucleic Acids Research
Nucleic acids research, vol 49, iss 15
Nucleic acids research, vol 49, iss 15
Architectural DNA-binding proteins (ADBPs) are abundant constituents of eukaryotic or bacterial chromosomes that bind DNA promiscuously and function in diverse DNA reactions. They generate large conformational changes in DNA upon binding yet can slid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e420ef7143198cda01c39efad7bd1282
http://europepmc.org/articles/PMC8421229
http://europepmc.org/articles/PMC8421229
Publikováno v:
PLoS ONE, Vol 11, Iss 3, p e0150189 (2016)
The abundant Fis nucleoid protein selectively binds poorly related DNA sequences with high affinities to regulate diverse DNA reactions. Fis binds DNA primarily through DNA backbone contacts and selects target sites by reading conformational properti
Externí odkaz:
https://doaj.org/article/49cd8a4abb7f44debb715330379431e7
Autor:
Satoshi Takahashi, Kana Ouchi, Yining Wu, Eriko Mano, Reid C. Johnson, Kiyoto Kamagata, Cheng Tan, Shoji Takada, Sridhar Mandali
Publikováno v:
Nucleic Acids Research
DNA binding proteins rapidly locate their specific DNA targets through a combination of 3D and 1D diffusion mechanisms, with the 1D search involving bidirectional sliding along DNA. However, even in nucleosome-free regions, chromosomes are highly dec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa9f4029419dab754f0f93473fcfe5bc
https://doi.org/10.1093/nar/gkaa799
https://doi.org/10.1093/nar/gkaa799
Autor:
Reid C. Johnson, Sridhar Mandali
Publikováno v:
Journal of bacteriology, vol 203, iss 16
J Bacteriol
J Bacteriol
Bacteriophage serine integrases catalyze highly specific recombination reactions between defined DNA segments called att sites. These reactions are reversible depending upon the presence of a second phage-encoded directionality factor. The bipartite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4a4aa043c5f375a8aeeda04fa6b5616
https://escholarship.org/uc/item/2s9253cj
https://escholarship.org/uc/item/2s9253cj
Multiple interfaces between a serine recombinase and an enhancer control site-specific DNA inversion
Publikováno v:
eLife, Vol 2 (2013)
Serine recombinases are often tightly controlled by elaborate, topologically-defined, nucleoprotein complexes. Hin is a member of the DNA invertase subclass of serine recombinases that are regulated by a remote recombinational enhancer element contai
Externí odkaz:
https://doaj.org/article/a0b0b822fc25465fa2295af9de4cb0ca
Publikováno v:
Nucleic Acids Research
Localized arrays of proteins cooperatively assemble onto chromosomes to control DNA activity in many contexts. Binding cooperativity is often mediated by specific protein–protein interactions, but cooperativity through DNA structure is becoming inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c18fe72b5d67de12420ea854e03f9e15
https://pubmed.ncbi.nlm.nih.gov/31616952
https://pubmed.ncbi.nlm.nih.gov/31616952
Publikováno v:
Journal of molecular biology, vol 430, iss 5
J Mol Biol
J Mol Biol
Architectural DNA-binding proteins function to regulate diverse DNA reactions and have the defining property of significantly changing DNA conformation. Although the 1D movement along DNA by other types of DNA-binding proteins has been visualized, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2229455005f25014629ebea78400bc54
https://escholarship.org/uc/item/2sf502x6
https://escholarship.org/uc/item/2sf502x6
Publikováno v:
Journal of bacteriology, vol 199, iss 11
The serine integrase of phage A118 catalyzes integrative recombination between attP on the phage and a specific attB locus on the chromosome of Listeria monocytogenes , but it is unable to promote excisive recombination between the hybrid attL and at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2ca6ae6bd008427c466bd302d3d7775
https://escholarship.org/uc/item/1423t03w
https://escholarship.org/uc/item/1423t03w