Hanson R L, Rose C
J Bacteriol. 1979 Jun;138(3):783-7. doi: 10.1128/jb.138.3.783-787.1979.
A mutation, pnt-1, causing loss of pyridine nucleotide transhydrogenase activity in Escherichia coli, was mapped by assaying for the enzyme in extracts of recombinant strains produced by conjugation, F-duction, and P1 transduction. The site of this mutation was near min 35, counterclockwise from man, and it co-transduced 59% with man. The mutation was associated with loss from the cell membrane fraction of energy-independent and adenosine 5'-triphosphate-dependent transhydrogenase activities, but reduced nicotinamide adenine dinucleotide dehydrogenase activity was not affected. Strains were constructed which lack phosphoglucoisomerase (pgi-2) and which carry either pnt+ or pnt-1. Although such strains, when grown on glucose, are expected to produce a large excess of reduced nicotinamide adenine dinucleotide phosphate, the growth rate was not affected by the pnt-1 allele.
通过检测由接合、F 因子转导和 P1 转导产生的重组菌株提取物中的酶活性,对大肠杆菌中导致吡啶核苷酸转氢酶活性丧失的突变体 pnt-1 进行了定位。该突变位点位于从 man 起逆时针方向约 35 分钟处,与 man 的共转导率为 59%。该突变与细胞膜部分中不依赖能量和依赖腺苷 5'-三磷酸的转氢酶活性丧失有关,但烟酰胺腺嘌呤二核苷酸磷酸还原酶活性未受影响。构建了缺乏磷酸葡萄糖异构酶(pgi-2)且携带 pnt+或 pnt-1 的菌株。尽管这些菌株在葡萄糖上生长时预计会产生大量过量的还原型烟酰胺腺嘌呤二核苷酸磷酸,但生长速率不受 pnt-1 等位基因的影响。