PMID:2226775
| Citation |
Sharrocks, AD, Green, J and Guest, JR (1990) In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E. coli. FEBS Lett. 270:119-22 |
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| Abstract |
FNR regulates the expression of target genes in response to anaerobiosis. It resembles the catabolite gene activator or cAMP-receptor protein (CRP) except for the presence of an N-terminal cysteine cluster, which may form a redox-sensing iron-binding site. Site-directed mutagenesis has shown that 3 of the 4 cysteine residues in the N-terminal cluster (Cys-20, -23 and -29, but not Cys-16) and the only other cysteine residue (Cys-122), are essential for the normal activation and repression of FNR-dependent promoters. Deletion of residues Pro-3-Arg-9 (inclusive) had no effect, but FNR was inactivated by a frameshift extending through the C-terminal DNA-binding domain. Four independent in vivo mutants contained identical Gly-96----Asp substitutions, which may inactivate FNR by distorting a sharp turn between beta-strands in the predicted structure. |
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| Keywords |
Amino Acid Sequence; Anaerobiosis/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Base Sequence; Chromosome Deletion; Cysteine; DNA-Binding Proteins/genetics; DNA-Binding Proteins/physiology; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Structure-Activity Relationship; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/physiology |
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