Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenlyase) operons in Escherichia coli
نویسندگان
چکیده
منابع مشابه
Molybdate binding by ModA, the periplasmic component of the Escherichia coli mod molybdate transport system.
ModA, the periplasmic-binding protein of the Escherichia coli mod transport system was overexpressed and purified. Binding of molybdate and tungstate to ModA was found to modify the UV absorption and fluorescence emission spectra of the protein. Titration of these changes showed that ModA binds molybdate and tungstate in a 1:1 molar ratio. ModA showed an intrinsic fluorescence emission spectrum...
متن کاملIn vitro incorporation of molybdate into demolybdoproteins in Escherichia coli.
When Escherichia coli was grown in the presence of tungstate, inactive forms of two molybdoenzymes, nitrate reductase and formate dehydrogenase, accumulated and were converted to their active forms upon incubation of cell suspensions with molybdate and chloramphenicol. The conversion to the active enzymes did not occur in cell extracts. When incubated with [(99)Mo]molybdate and chloramphenicol,...
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I,-Arabinosr is transported into Escherichia coli via two independent transport systems, a system possessing relatively low affinity for arabinose, the araE system, and a system of higher affinity for arabinose, t)he araFG system. In the work reported here we demonstrate that insert,ion of the Mu-Zac bacteriophage isolated by Casadaban 8r Cohen (1979) permits a reliable measurement’ of the expr...
متن کاملPhenotypic Restoration by Molybdate of Nitrate
ChlD mutants of Escherichia coli are pleiotropic, lacking formate-nitrate reductase activity as well as formate-hydrogenlyase activity. Whole-chain formate-nitrate reductase activity, assayed with formate as the electron donor and measuring the amount of nitrite produced, was restored to wild-type levels in the mutants by addition of 10-4 M molybdate to the growth medium. Under these conditions...
متن کاملGenetic analysis of the modABCD (molybdate transport) operon of Escherichia coli.
DNA sequence analysis of the modABCD operon of Escherichia coli revealed the presence of four open reading frames. The first gene, modA, codes for a 257-amino-acid periplasmic binding protein enunciated by the presence of a signal peptide-like sequence. The second gene (modB) encodes a 229-amino-acid protein with a potential membrane location, while the 352-amino-acid ModC protein (modC product...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1995
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.177.17.4857-4864.1995