Abstract:
:The response regulator proteins of two-component systems mediate many adaptations of bacteria to their ever-changing environment. Most response regulators are transcription factors that alter the level of transcription of specific sets of genes. Activation of response regulators requires their phosphorylation on a conserved aspartate residue by a cognate sensor kinase. For this reason, expression of a recombinant response regulator in the absence of the requisite sensor kinase is expected to yield an unphosphorylated product in the inactive state. For Spo0A, the response regulator controlling sporulation in Bacillus subtilis however, we have found that a significant fraction of the purified recombinant protein is phosphorylated. This phosphorylated component is dimeric and binds to Spo0A recognition sequences in DNA. Treatment with the Spo0A-specific phosphatase, Spo0E, leads to dissociation of the dimers and loss of DNA binding. It is therefore necessary to pre-treat recombinant Spo0A preparations with the cognate phosphatase, to generate the fully inactive state of the molecule.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Ladds JC,Muchová K,Blaskovic D,Lewis RJ,Brannigan JA,Wilkinson AJ,Barák Idoi
10.1016/S0378-1097(03)00321-5keywords:
subject
Has Abstractpub_date
2003-06-27 00:00:00pages
153-7issue
2eissn
0378-1097issn
1574-6968pii
S0378109703003215journal_volume
223pub_type
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