Pleiotropic effect of his gene mutations on nitrogen fixation in Klebsiella pneumoniae

TY - JOUR

T1 - Pleiotropic effect of his gene mutations on nitrogen fixation in Klebsiella pneumoniae

AU - Jensen, Jens Stougaard

AU - Kennedy, C

PY - 1982

Y1 - 1982

N2 - Several his mutations were found to influence nitrogen fixation in Klebsiella pneumoniae: hisB, hisC, and hisD mutants had 50% of wild-type levels of nitrogenase activity when supplied with 30 mug or less histidine/ml although this concentration did not limit protein synthesis and the mutants retained a Nif plate phenotype. A hisA mutation had a similar but more dramatic effect. At low concentrations of histidine the hisA mutant strain had only 5% of the nitrogenase activity found at high histidine concentration or in a his strain, and was also Nif on low histidine agar plates. Addition of adenine restored nitrogenase activity in the hisA but not the hisB, hisC, or hisD mutants. Low levels of intracellular ATP, a consequence of hisG enzyme activity, correlated with loss of nitrogen-fixing ability in the hisA mutant which failed to sustain nif gene expression under these conditions. Synthesis of other major cell proteins was relatively unaffected indicating that nif gene expression is selectively regulated by the energy status of the organism.

AB - Several his mutations were found to influence nitrogen fixation in Klebsiella pneumoniae: hisB, hisC, and hisD mutants had 50% of wild-type levels of nitrogenase activity when supplied with 30 mug or less histidine/ml although this concentration did not limit protein synthesis and the mutants retained a Nif plate phenotype. A hisA mutation had a similar but more dramatic effect. At low concentrations of histidine the hisA mutant strain had only 5% of the nitrogenase activity found at high histidine concentration or in a his strain, and was also Nif on low histidine agar plates. Addition of adenine restored nitrogenase activity in the hisA but not the hisB, hisC, or hisD mutants. Low levels of intracellular ATP, a consequence of hisG enzyme activity, correlated with loss of nitrogen-fixing ability in the hisA mutant which failed to sustain nif gene expression under these conditions. Synthesis of other major cell proteins was relatively unaffected indicating that nif gene expression is selectively regulated by the energy status of the organism.

KW - Journal Article

M3 - Journal article

C2 - 16453412

SN - 0261-4189

VL - 1

SP - 197

EP - 204

JO - E M B O Journal

JF - E M B O Journal

IS - 2

ER -