Structure of the nifQ gene from Enterobacter agglomerans 333 and its overexpression in Escherichia coli

Siddavattam, Dayananda ; Singh, Mahavir ; Klingmuller, Walter (1993) Structure of the nifQ gene from Enterobacter agglomerans 333 and its overexpression in Escherichia coli Molecular & General Genetics, 239 (3). pp. 435-440. ISSN 0026-8925

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Official URL: https://link.springer.com/article/10.1007/BF002769...

Related URL: http://dx.doi.org/10.1007/BF00276942

Abstract

The nifQ gene, involved in early stages of iron-molybdenum cofactor (FeMo-co) biosynthesis, was identified downstream of the nijB and nijF genes of Enterobacter agglomerans. This gene was cloned and its nucleotide sequence determined. The amino acid sequence, as deduced from the nucleotide sequence, revealed an accumulation of cysteine amino acid residues at the C-terminal end of the protein. The cysteine cluster showed the following consensus sequence Cys-X4-Cys-X2-Cys-X5-Cys, which is a typical characteristic of metal-binding proteins. Further, the nifQ gene was cloned downstream of strong transcriptional (bacteriophage λpLpR) and translational (atpE) signals of the expression vector pCYTEXP1 and expressed as an unfused, soluble protein in Escherichia coli. The molecular mass of 19 kDa, as deduced by SIDS-PAGE, is in good agreement with the molecular mass deduced from the nucleotide sequence. The availability of high-level expression clones should facilitate purification of large quantities of the recombinant NifQ protein and elucidation of its properties.

Item Type:Article
Source:Copyright of this article belongs to Springer Verlag.
Keywords:Enterobacter Agglomerans; nifQ; Gene; Femo-cofactor; Nitrogen Fixation; Overexpression
ID Code:114187
Deposited On:28 May 2018 08:22
Last Modified:28 May 2018 08:22

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