The Alcaligenes eutrophus protein HoxN mediates nickel transport in Escherichia coli
نویسندگان
چکیده
منابع مشابه
The Alcaligenes eutrophus protein HoxN mediates nickel transport in Escherichia coli.
HoxN, an integral membrane protein with seven transmembrane helices and a molecular mass of 33.1 kDa, is involved in high-affinity nickel transport in Alcaligenes eutrophus H16. From genetic analyses, it has been concluded that HoxN is a single-component ion carrier. To investigate this assumption, hoxN was introduced into Escherichia coli. The recombinant strain showed significantly enhanced n...
متن کاملNickel requirement for active hydrogenase formation in Alcaligenes eutrophus.
The nickel-dependent chemolithoautotrophic growth of Alcaligenes eutrophus is apparently due to a requirement of nickel for active hydrogenase formation. Cells grown heterotrophically with fructose and glycerol revealed a specific activity of soluble and membrane-bound hydrogenase which was severalfold higher than the normal autotrophic level. The omission of nickel from the medium did not affe...
متن کاملExpression of the Escherichia coli pfkA gene in Alcaligenes eutrophus and in other gram-negative bacteria.
The Escherichia coli pfkA gene has been cloned in the non-self-transmissible vector pVK101 from hybrid plasmids obtained from the Clarke and Carbon clone bank, resulting in the plasmids pAS300 and pAS100; the latter plasmid also encoded the E. coli tpi gene. These plasmids were transferred by conjugation to mutants of Alcaligenes eutrophus which are unable to grow on fructose and gluconate due ...
متن کاملRegulated expression of the Alcaligenes eutrophus pha biosynthesis genes in Escherichia coli.
A novel poly-beta-hydroxybutyrate (PHB) production system in which the expression and gene dosage of the Alcaligenes eutrophus pha biosynthetic operon were effectively regulated by cultivation temperature was constructed in Escherichia coli. The pha operon was fused to the negatively regulated tac promoter and cloned into a vector in which the copy number is temperature dependent. A two-phase p...
متن کاملA Ni2+ binding motif is the basis of high affinity transport of the Alcaligenes eutrophus nickel permease.
Amino acid exchanges in the Alcaligenes eutrophus nickel permease (HoxN) were constructed by site-directed mutagenesis, and their effects on nickel ion uptake were investigated. Mutant hoxN alleles were expressed in Escherichia coli, and activity of the altered permeases was examined via a recently described physiological assay (Wolfram, L., Friedrich, B., and Eitinger, T. (1995) J. Bacteriol. ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1995
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.177.7.1840-1843.1995