Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Ajit K, Satapathy"'
Publikováno v:
Journal of Biological Chemistry. 286:23113-23120
The DNA helicase encoded by gene 4 of bacteriophage T7 forms a hexameric ring in the presence of dTTP, allowing it to bind DNA in its central core. The oligomerization also creates nucleotide-binding sites located at the interfaces of the subunits. D
Publikováno v:
Journal of Biological Chemistry. 284:14286-14295
The multifunctional protein encoded by gene 4 of bacteriophage T7 (gp4) provides both helicase and primase activity at the replication fork. T7 DNA helicase preferentially utilizes dTTP to unwind duplex DNA in vitro but also hydrolyzes other nucleoti
Autor:
Sumana Bhattacharjya, M. K. Ray, Theetha L. Pavankumar, Ajit K. Satapathy, Rajan Sankaranarayanan
Publikováno v:
FEBS Journal. 275:1835-1851
RecD is essential for growth at low temperature in the Antarctic psychrotrophic bacterium Pseudomonas syringae Lz4W. To examine the essential nature of its activity, we analyzed wild-type and mutant RecD proteins with substitutions of important resid
Publikováno v:
Genetics. 170:1473-1484
The Antarctic psychrotrophic bacterium Pseudomonas syringae Lz4W has been used as a model system to identify genes that are required for growth at low temperature. Transposon mutagenesis was carried out to isolate mutant(s) of the bacterium that are
Publikováno v:
The FASEB Journal. 25
Autor:
Arkadiusz W. Kulczyk, Antoine M. van Oijen, Sharmistha Ghosh, Charles C. Richardson, Ajit K. Satapathy
Publikováno v:
J. Biol. Chem., 286(39), 34468-34478. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
The DNA helicase encoded by gene 4 of bacteriophage T7 assembles on single-stranded DNA as a hexamer of six identical subunits with the DNA passing through the center of the toroid. The helicase couples the hydrolysis of dTTP to unidirectional transl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47cdf8394436191cd212f2052c8d24b9
https://research.rug.nl/en/publications/4a9a6858-71f9-44cf-9408-232d313eead0
https://research.rug.nl/en/publications/4a9a6858-71f9-44cf-9408-232d313eead0
Autor:
Antoine M. van Oijen, Ajit K. Satapathy, Anna B. Kochaniak, Donald J. Crampton, Charles C. Richardson, Swagata Mukherjee
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 107(15), 6782-6787. NATL ACAD SCIENCES
The ring-shaped helicase of bacteriophage T7 (gp4), the product of gene 4, has basic β-hairpin loops lining its central core where they are postulated to be the major sites of DNA interaction. We have altered multiple residues within the β-hairpin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84bf446879481a19c1cf2d494ff79559
https://europepmc.org/articles/PMC2872414/
https://europepmc.org/articles/PMC2872414/
Publikováno v:
The Journal of biological chemistry. 284(21)
The multifunctional protein encoded by gene 4 of bacteriophage T7 (gp4) provides both helicase and primase activity at the replication fork. T7 DNA helicase preferentially utilizes dTTP to unwind duplex DNA in vitro but also hydrolyzes other nucleoti
Autor:
Ajit K, Satapathy, Theetha L, Pavankumar, Sumana, Bhattacharjya, Rajan, Sankaranarayanan, Malay K, Ray
Publikováno v:
The FEBS journal. 275(8)
RecD is essential for growth at low temperature in the Antarctic psychrotrophic bacterium Pseudomonas syringae Lz4W. To examine the essential nature of its activity, we analyzed wild-type and mutant RecD proteins with substitutions of important resid