In vitro DNA binding of purified CcpA protein from Lactococcus lactis IL1403

• Autorzy: Kowalczyk M. , Borcz B. , Plochocka D. , Bardowski J.
• Języki publikacji: EN

Abstrakty

EN

During this study His-tagged CcpA protein purified under native conditions to obtain a biologically active protein was used for molecular analysis of CcpA-dependent regulation. Using electrophoretic mobility shift assays it was demonstrated that CcpA of L. lactis can bind DNA in the absence of the HPr-Ser-P corepressor and exhibits DNA-binding affinity for nucleotide sequences lacking cre sites. However, purified HPr-Ser-P protein from Bacillus subtilis was shown to slightly increase the DNA-binding capacity of the CcpA protein. It was also observed that CcpA bound to the cre box forms an apparently more stable complex than that resulting from unspecific binding. Competition gel retardation assay performed on DNA sequences from two PEP:PTS regions demonstrated that the ybhE, bglS, rheB, yebE, ptcB and yecA genes situated in these regions are most probably directly regulated by CcpA.

Słowa kluczowe

EN

DNA sequence; bglS gene; bovine serum albumin; ybhE gene; Gram-positive bacterium; electrophoretic mobility shift assay; carbon catabolite repression; DNA binding; rheB gene; Bacillus subtilis; in vitro; competition; CcpA protein; ptcB gene; yecA gene; yebE gene; Lactococcus lactis; bacteria

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2007
• Tom: 54
• Numer: 1
• Opis fizyczny: p.71-78,fig.,ref.

Twórcy

autor

Kowalczyk M.

• Polish Academy of Sciences, A.Pawinskiego 5a, 02-106 Warsaw, Poland

autor

Borcz B.

autor

Plochocka D.

autor

Bardowski J.

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