Premium
Critical spacing between two essential cysteine residues in the interdomain linker of the Bradyrhizobium japonicum NifA protein
Author(s) -
Fischer Hans-Martin,
Fritsche Stefan,
Herzog Brigitte,
Hennecke Hauke
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81083-x
Subject(s) - cysteine , linker , chemistry , bradyrhizobium japonicum , bradyrhizobium , biochemistry , biology , bacteria , genetics , computer science , rhizobiaceae , enzyme , gene , symbiosis , rhizobium , operating system
A special sequence motif in the Bradyrhizobium japonicum NifA protein, consisting of two functionally essential cysteines separated by four other amino acids (Cys‐aa 4 ‐Cys), has been proposed to be part of a potential metal‐binding site [(1988) Nucleic Acids Res. 16, 2207–2224]. Using the techniques of oligonucleotide‐directed mutagenesis, we report here that several of the four intervening amino acids can be replaced by others without loss of NifA function. The deletion of one amino acid to give a Cys‐aa 3 ‐Cys motif renders the protein inactive whereas the creation of a Cys‐aa 5 ‐Cys motif (one amino acid inserted) still leads to a partially active NifA protein.