Crystallization and preliminary X-ray analysis of the sporulation factor SpoIIAA in its native and phosphorylated forms
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作者:
Seavers, PR
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Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, EnglandUniv York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England
Seavers, PR
[1
]
Lewis, RJ
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Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, EnglandUniv York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England
Lewis, RJ
[1
]
Brannigan, JA
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Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, EnglandUniv York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England
Brannigan, JA
[1
]
Wilkinson, AJ
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Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, EnglandUniv York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England
Wilkinson, AJ
[1
]
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[1] Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England
Sporulation in Bacillus begins with an asymmetric cell division producing two progeny with identical chromosomes but different developmental fates. As such, it is a simple example of cellular differentiation. The establishment of cell type is controlled by a series of alternate RNA polymerase sigma subunits. The first compartment-specific sigma factor is sigma (F), whose activity is controlled by SpoIIAB, an anti-sigma factor, and SpoIIAA, an anti-sigma factor antagonist which is phosphorylated by the kinase activity of SpoIIAB. Here, the preliminary crystallographic analysis of SpoIIAA and phosphorylated SpoIIAA from B. sphaericus in forms suitable for high-resolution structure determination are reported.