Open AccessThe N-terminal part of theE.ColiDNA binding protein FIS is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding
Author(s) -
Christian A. Koch,
Olaf Ninnemann,
Heidemarie Fuss,
Regine Kahmann
Publication year - 1991
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/19.21.5915
Subject(s) - biology , dna , microbiology and biotechnology , operon , enhancer , mutant , gene , dna binding site , transcription (linguistics) , dna binding protein , genetics , gene expression , transcription factor , promoter , linguistics , philosophy
FIS protein is involved in several different cellular processes stimulating site-specific recombination in phages Mu and lambda as well as transcription of stable RNA operons in E.coli. We have performed a mutational analysis of fis and provide genetic and biochemical evidence that a truncated version of FIS lacking the N-terminal region is sufficient for specific DNA binding and for stimulating lambda excision. These mutants also retain their ability to autoregulate fis gene expression. Such mutant proteins, however, cannot stimulate the enhancer dependent DNA inversion reaction.