Abstract：
:Adenosine cyclic 3',5'-phosphate receptor protein (CRP or CAP) is a regulatory protein involved in the transcription of several operons in Escherichia coli. cAMP-independent, nonspecific complexes of CRP and DNA were investigated by photochemical cross-linking of the protein to nonspecific DNA, whose thymines are substituted by 5-bromouracil (BrUra). The cross-linked protein was completely digested by trypsin, and the covalently bound peptides were sequenced. We identified two regions of the protein in close contact with DNA: one in the C-terminal part, overlapping the canonical helix-turn-helix motif, and the other one in the N-terminal part, which is usually not considered to belong to the DNA-interacting domain of CRP. This result lead us to propose models for nonspecific interaction, where the DNA is in contact with both the N- and C-terminal parts of the protein.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Katouzian-Safadi M,Blazy B,Cremet JY,Le Caer JP,Rossier J,Charlier Mdoi
10.1021/bi00058a010subject
Has Abstractpub_date
1993-02-23 00:00:00pages
1770-3issue
7eissn
0006-2960issn
1520-4995journal_volume
32pub_type
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