Identification of the DNA-binding protein, HrcA, of Streptococcus thermophilus.
HrcA is a negative transcriptional factor controlling the expression of the stress-specific operons dnaK and groESL in several bacteria. Although the HrcA structural gene has been identified in various organisms, studies at the protein level have been so far limited and mostly restricted to Bacillus subtilis. We have identified the HrcA protein of Streptococcus thermophilus and show here that it is a dimer with a native molecular mass of 74.5 kDa and a sequence-specific DNA-binding activity. Partially denatured and inactive S. thermophilus HrcA recovered its binding activity in the presence of the GroEL chaperone.
Martirani
L
L
Department of General and Environmental Physiology, University Federico II, Naples, Italy.
Raniello
R
R
Naclerio
G
G
Ricca
E
E
De Felice
M
M
D001412:Bacillus subtilis / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites; D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism; D016384:Consensus Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019281:Dimerization; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics; D008970:Molecular Weight; D009876:Operon; D011489:Protein Denaturation; D020673:Protein Renaturation; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D013291:Streptococcus / Q000235:genetics* / Q000378:metabolism*
D001426:Bacterial Proteins; D018834:Chaperonin 60; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D012097:Repressor Proteins; C063842:dnaK protein, E coli