دورية أكاديمية

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

التفاصيل البيبلوغرافية
العنوان: Cloning, expression and sequencing the molybdenum-pterin binding protein (mop) gene of Clostridium pasteurianum in Escherichia coli.
المؤلفون: Hinton SM, Freyer G
المصدر: Nucleic acids research [Nucleic Acids Res] 1986 Dec 09; Vol. 14 (23), pp. 9371-80.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print Cited Medium: Print ISSN: 0305-1048 (Print) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
أسماء مطبوعة: Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
مواضيع طبية MeSH: Cloning, Molecular* , Coenzymes* , Genes, Bacterial* , Metalloproteins*, Bacterial Proteins/*genetics , Carrier Proteins/*genetics , Clostridium/*genetics , Escherichia coli/*genetics , Molybdenum/*metabolism , Pteridines/*metabolism, Amino Acid Sequence ; Bacterial Proteins/analysis ; Bacterial Proteins/physiology ; Base Sequence ; Carrier Proteins/analysis ; Carrier Proteins/physiology ; Chromosome Mapping ; DNA, Bacterial/analysis ; DNA-Binding Proteins/analysis ; Molybdenum Cofactors ; Pterins
مستخلص: 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.
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سلسلة جزيئية: GENBANK X04982
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Carrier Proteins)
0 (Coenzymes)
0 (DNA, Bacterial)
0 (DNA-Binding Proteins)
0 (Metalloproteins)
0 (Molybdenum Cofactors)
0 (Pteridines)
0 (Pterins)
0 (mopI protein, Clostridium pasteurianum)
81AH48963U (Molybdenum)
ATN6EG42UQ (molybdenum cofactor)
تواريخ الأحداث: Date Created: 19861209 Date Completed: 19870218 Latest Revision: 20211203
رمز التحديث: 20221208
مُعرف محوري في PubMed: PMC311964
DOI: 10.1093/nar/14.23.9371
PMID: 3540853
قاعدة البيانات: MEDLINE