Open AccessAn additional P II in Escherichia coli : a new regulatory protein in the glutamine synthetase cascade
Author(s) -
Heeswijk Wally C.,
Stegeman Brenda,
Hoving Sjouke,
Molenaar Douwe,
Kahn Daniel,
Westerhoff Hans V.
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07825.x
Subject(s) - escherichia coli , glutamine synthetase , biology , glutamine , biochemistry , tyrosine , peptide sequence , amino acid , enterobacteriaceae , dna , microbiology and biotechnology , gene
The P II protein in the glutamine synthetase cascade transduces the nitrogen signal, as sensed by uridylyltransferase, both to the NRII/NRI two‐component system and to adenylyltransferase, to regulate the activity of glutamine synthetase. Here we describe the amplification of a chromosomal DNA fragment from Escherichia coli which contains the sequence of a P II homologue. The derived amino acid sequence of this DNA fragment is 67% identical to E. coli P II . It contains the conserved tyrosine residue which is known to be the site of uridylylation in P II . E. coli is the first organism in which two different P II proteins have been detected.