Potential for selection among nearly neutral allozymes of 6-phosphogluconate dehydrogenase in Escherichia coli.
نویسندگان
چکیده
منابع مشابه
Selective neutrality of glucose-6-phosphate dehydrogenase allozymes in Escherichia coli.
Six naturally occurring alleles representing four electromorphs of the enzyme glucose-6-phosphate dehydrogenase were transferred by P1-mediated transduction from natural isolates of Escherichia coli into the genetic background of E. coli K12 and were studied in pairwise competition in chemostats limited for glucose in order to estimate differences in growth rate associated with the alleles. Alt...
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A novel genetic change leading to increased activity of 6-phosphogluconate dehydrogenase (6PGD) in E. coli has been observed. The mutation is a deletion of approximately 0 .4 kilobase pairs occurring between the structural gene of GPGD ( g n d ) and one copy of an insertion element (IS5) found normally in E. coli K 12 a few hundred base pairs upstream (counterclockwise) from gnd at 44 minutes o...
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Two crystal structures of recombinant Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase (Gs6PDH) in complex with the substrate 6-phosphogluconate have been determined at medium resolution. Gs6PDH shares significant sequence identity and structural similarity with the enzymes from Lactococcus lactis, sheep liver and the protozoan parasite Trypanosoma brucei, for which a range of st...
متن کاملSelective neutrality of 6PGD allozymes in E. coli and the effects of genetic background.
We have used gluconate-limited chemostats to study selective differences between isogenic strains of Escherichia coli K12 into which four naturally occurring alleles coding for allozymes of 6-phosphogluconate dehydrogenase (6PGD) had been transferred. The limit of detectability of selection with our procedures is a selection coefficient of 0.5%. In the normal E. coli K12 genetic background, all...
متن کاملOverexpression and simple purification of the Thermotoga maritima 6-phosphogluconate dehydrogenase in Escherichia coli and its application for NADPH regeneration
BACKGROUND Thermostable enzymes from thermophilic microorganisms are playing more and more important roles in molecular biology R&D and industrial applications. However, over-production of recombinant soluble proteins from thermophilic microorganisms in mesophilic hosts (e.g. E. coli) remains challenging sometimes. RESULTS An open reading frame TM0438 from a hyperthermophilic bacterium Thermo...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1981
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.78.10.6344