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of 4
pro vyhledávání: '"Stephen N. Abbott"'
Publikováno v:
Journal of Biological Chemistry. 281:12968-12975
The RecA residues Lys248 and Glu96 are closely opposed across the RecA subunit-subunit interface in some recent models of the RecA nucleoprotein filament. The K248R and E96D single mutant proteins of the Escherichia coli RecA protein each bind to DNA
Autor:
Jong-Il Kim, Michael M. Cox, Ross B. Inman, Stephen N. Abbott, Aaron Jambura, David W. Dwyer, Ajay K. Sharma, Elizabeth A. Wood, Michael J. Daly, Kenneth W. Minton
Publikováno v:
Journal of Bacteriology. 184:1649-1660
The RecA protein of Deinococcus radiodurans (RecA Dr ) is essential for the extreme radiation resistance of this organism. The RecA Dr protein has been cloned and expressed in Escherichia coli and purified from this host. In some respects, the RecA D
Publikováno v:
Virology. 260(1):64-73
Proper formation of the bacteriophage T4 DNA polymerase holoenzyme requires a wide spectrum of protein–protein and protein–DNA interactions among the DNA polymerase gp43, the sliding clamp gp45, and gp44/62, the clamp loader complex (CLC). The 44
Publikováno v:
The Journal of biological chemistry. 281(18)
The RecA residues Lys248 and Glu96 are closely opposed across the RecA subunit-subunit interface in some recent models of the RecA nucleoprotein filament. The K248R and E96D single mutant proteins of the Escherichia coli RecA protein each bind to DNA