Zobrazeno 1 - 10 of 32 pro vyhledávání: '"Mark Levinthal"'
2
The H-NS protein modulates the activation of the ilvIH operon of Escherichia coli K12 by Lrp, the leucine regulatory protein
Autor: Antoine Danchin, Mark Levinthal, Philippe Lejeune
Publikováno v: Molecular and General Genetics MGG. 242:736-743
The H-NS protein, the product of the hns gene, plays a central role in the cellular response of bacteria to environmental stresses such as modification of osmolarity and temperature. The leucine regulatory protein (Lrp) controls a wide array of opero
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66ec828c72f522750f063057e58a67b8
https://doi.org/10.1007/bf00283429
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3
The role of H-NS in one carbon metabolism
Autor: Mark Levinthal, Antoine Danchin, J.R. Landgraf
Publikováno v: Biochimie. 76:1063-1070
The H-NS protein of Escherichia coli regulates the expression of genes involved in many general processes such as osmoregulation and virulence. More recently, H-NS was shown to exert an effect on ilvIH gene expression in conjunction with the leucine
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4bbb5b9f0bfa10bdf4d3b7d2e391272
https://doi.org/10.1016/0300-9084(94)90031-0
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5
Specific binding of the first enzyme for histidine biosynthesis to the DNA of the histidine operon
Autor: Tikvah Vogel, Robert F. Goldberger, John S. Kovach, Mark Levinthal, Carmelo B. Bruni, Marilyn Meyers, Kathleen P. Mullinix, Roger G. Deeley, Francesco Blasi
Publikováno v: Nucleic Acids Research. 2:2021-2036
Studies were done to examine direct binding of the first enzyme of the histidine biosynthetic pathway (phosphoribosyltransferase) to 32P-labeled phi80dhis DNA and competition of this binding by unlabeled homologous DNA and by various preparations of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04c54ad16d17d5e19a159f2583f304a6
https://doi.org/10.1093/nar/2.11.2021
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6
Reversion of the effects of a threonine deaminase regulatory mutant by a mutation in ilvH in Escherichiacoli K-12
Autor: Phillip A. Singer, Luther S. Williams, Mark Levinthal
Publikováno v: Biochemical and Biophysical Research Communications. 118:270-277
In a strain carrying an ilvA538 mutation, the ilvGEDA operon expression is decreased (hyperattenuated) and the activity and/or expression of isoleucyl- and valyl- tRNA synthetases is decreased. We have isolated two revertants of ilvA538 owing to muta
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7daab54568c5ebbc475b283cdaf14b1b
https://doi.org/10.1016/0006-291x(84)91096-9
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7
Regulation of synthesis of the acetohydroxy acid synthase I isoenzyme in Escherichia coli K-12
Autor: Maurilio De Felice, Mark Levinthal, Thomas C. Newman
Publikováno v: Biochimica et Biophysica Acta (BBA) - General Subjects. 541:1-8
We studied derivatives of Escherichia coli K-12 expressing only one of the three acetohydroxy acid synthases, acetohydroxy acid synthase I (the ilvB gene product), to gain insight into the mechanism of synthesis of this isoenzyme. We found that aceto
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80362c6342c45fdcb45e3b3ec72408d0
https://doi.org/10.1016/0304-4165(78)90262-3
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8
The regulation of the ilvADGE operon: Evidence for positive control by threonine deaminase
Autor: Luther S. Williams, Mark Levinthal, Maxine Levinthal
Publikováno v: Journal of Molecular Biology. 102:453-465
We isolated a strain (PS187) containing a mutation in the ilvA structural gene (threonine deaminase) affecting the regulation of the isoleucine and valine biosynthetic enzymes. We studied the effect of the mutation, ilvA538, on the ability of the ilv
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::346e1a67cad379d5712facc698516b0f
https://doi.org/10.1016/0022-2836(76)90327-2
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9
Metabolic interlock between the acetolactate synthase isoenzymes and lysine biosynthesis in Escherichia coli K-12
Autor: Maurizio Iaccarino, John Guardiola, Werner Schreil, Maurilio De Felice, Mark Levinthal
Publikováno v: Molecular and General Genetics MGG. 156:9-16
Some of the strains containing mutations in the genes for the acetolactate synthase isoenzymes are temperature sensitive (ts). Suppression of the acetolactate synthase defect due to one of these mutations suppresses also the ts phenotype; moreover, a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::762af42153a825a7e7b916622248083e
https://doi.org/10.1007/bf00272246
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10
Synthesis of the isoleucyl- and valyl-tRNA synthetases and the isoleucine-valine biosynthetic enzymes in a threonine deaminase regulatory mutant of Escherichia coli K-12
Autor: Phillip A. Singer, Luther S. Williams, Mark Levinthal
Publikováno v: Journal of Molecular Biology. 175:39-55
A mutation in the structural gene for threonine deaminase, ilvA538 , results in lower than normal levels of the isoleucyl, valyl- and leucyl-tRNA synthetases. Moreover, this regulatory mutation decreases the level of expression of the ilv biosyntheti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb8062eef901f3b1a5739dee2c4d4443
https://doi.org/10.1016/0022-2836(84)90444-3
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