Effect of mutations affecting lysyl-tRNAlys on the regulation of lysine biosynthesis in Escherichia coli. |
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Authors: | Emmanuelle Boy Françoise Borne and Jean-Claude Patte |
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Institution: | (1) Institut de Microbiologie, Université Paris-Sud, Centre d'Orsay, F-91405 Orsay, France |
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Abstract: | Summary When studying mutants affecting lysyl-tRNA synthetase or tRNALys (hisT, hisW), a lack of correlation is clearly observed between the amount of lysyl-tRNA and the level of derepression of several lysine biosynthetic enzymes. This excludes the possible role of lysyl-tRNA as the specific corepressor of the lysine regulon. However, the level of derepression of DAP-decarboxylase, the last enzyme of the lysine pathway, is very low in the hisT mutant; this indicates that tRNALys is a secondary effector involved in the regulation of the synthesis of this enzyme.Abbreviations DAP
diaminopimelate
- KRS
lysyl-tRNA synthetase
- L-lysine
tRNA ligase (AMP) (EC6.1.16)
- AK III
lysinesensitive aspartokinase (EC 2.7.24)
- ASA-dehydrogenase
aspartic semialdehyde dehydrogenase (EC 1.2.1.10)
- DHDP-reductase
dihydrodipicolinic acid reductase
- DAP-decarboxylase
diaminopimelate decarboxylase (EC 4.1.1.20)
- AK I
threonine-sensitive aspartokinase
- HDHI
threonine-sensitive homoserine dehydrogenase |
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