Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Sridhar Mandali"'
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
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
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
Autor:
Philipp Verpukhovskiy, Leonid Kruglyak, Tzitziki Lemus-Vergara, Eyal Ben-David, Sridhar Mandali, Pinelopi Pliota, Alejandro Burga, Christian Braendle, Alevtina Koreshova, Sonya A. Widen
Publikováno v:
Current Biology
Summary Toxin-antidote elements (TAs) are selfish genetic dyads that spread in populations by selectively killing non-carriers. TAs are common in prokaryotes, but very few examples are known in animals. Here, we report the discovery of maternal-effec
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
Publikováno v:
Virology. 408:64-70
Phage integrases have the potential of becoming tools for safe site-specific integration of genes into unmodified human genomes. The P2-like phages have been found to have different bacterial host integration sites and consequently they have related
Publikováno v:
Mandali, Sridhar; Dhar, Gautam; Avliyakulov, Nuraly K; Haykinson, Michael J; & Johnson, Reid C. (2013). The site-specific integration reaction of Listeria phage A118 integrase, a serine recombinase. Mobile DNA, 4(1), 2. doi: http://dx.doi.org/10.1186/1759-8753-4-2. Retrieved from: http://www.escholarship.org/uc/item/49c711v2
Mobile DNA
Mobile DNA, Vol 4, Iss 1, p 2 (2013)
Mobile DNA
Mobile DNA, Vol 4, Iss 1, p 2 (2013)
Background A large subfamily of serine recombinases contains long polypeptide segments appended to the C-terminal end of the conserved catalytic domain. Members of this subfamily often function as phage integrases but also mediate transposition and r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1afbf906a00489212b78df4203cd4be
http://www.escholarship.org/uc/item/49c711v2
http://www.escholarship.org/uc/item/49c711v2
Autor:
Jesper M. Eriksson, Wilhelmina Sehlén, Lina Sylwan, Carlos Cardoso-Palacios, Alexandra Ahlgren-Berg, Elisabeth Haggård-Ljungquist, Sridhar Mandali
Publikováno v:
Virology. (2):303-312
The Cox protein of the coliphage P2 is multifunctional; it acts as a transcriptional repressor of the Pc promoter, as a transcriptional activator of the P LL promoter of satellite phage P4, and as a directionality factor for site-specific recombinati