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Nucleic Acids Research, 1986, Vol. 14, No. 23 9371-9380
© 1986

Articles

Cloning, expression and sequencing the molybdenum-pterin binding protein (mop) gene of Clostridium pasteurianum in Escherichia coli

Stephen M. Hinton* and Greg Freyer1,+

Exxon Liaison Inc., Cold Spring Harbor NY 11724, USA 1Cold Spring Harbor Laboratory, Cold Spring Harbor NY 11724, USA

*To whom correspondence should be addressed

Received September 9, 1986. Accepted November 4, 1986.

mop is the structural gene for the molybdenum-pterin binding protein, which is the major molybdenum binding protein in Clostridium pastuerianum. The mop gene was detected by immunoscreening genomic libraries of C pastuerianum and identified by determining the nucleotide sequence of the cloned insert of clostridial DNA. The deduced amino acid sequence of an open reading frame proved to be identical to the first twelve residues of purified Mop. The DNA sequence flanking the mop gene contains promoter-like consensus sequences which are probably responsible for the expression of Mop in Escherichia coli. The deduced amino acid composition shows that the protein is hydrophobic, lacks aromatic and cysteine residues and has a calculated molecular weight of 7, 038. The N-terminal amino acid sequence of Mop has sequence homology with DNA binding proteins. The pattern and type of residues in the N-terminal region suggest it forms the helix-turn-helix structure observed in DNA binding proteins. We propose that Mop may be a regulatory protein binding the anabolic source of molybdenum.

+present address: Sloan-Kettering, New York, NY 10021, USA


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