Glutamine synthetase of Klebsiella aerogenes: properties of glnD mutants lacking uridylyltransferase
Author(s) -
F Foor,
Robert Cedergren,
S L Streicher,
Sue Goo Rhee,
Boris Magasanik
Publication year - 1978
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.134.2.562-568.1978
Subject(s) - glutamine synthetase , adenylylation , biology , enterobacter aerogenes , glutamine , mutant , biochemistry , mutation , klebsiella pneumoniae , enzyme , gene , microbiology and biotechnology , biosynthesis , escherichia coli , amino acid
The glnD mutation of Klebsiella aerogenes is cotransducible by phage P1 with pan (requirement for pantothenate) and leads to a loss of uridylytransferase and uridylyl-removing enzyme, components of the glutamine synthetase adenylylation system. This defect results in an inability to deadenylylate glutamine synthetase rapidly and in a requirement for glutamine for normal growth. Suppression of the glnD mutation are located at the glutamine synthetase structural gene glnA.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom