Literature DB >> 3018439

Conservation of primary structure in the hisI gene of the archaebacterium, Methanococcus vannielii, the eubacterium Escherichia coli, and the eucaryote Saccharomyces cerevisiae.

G S Beckler, J N Reeve.   

Abstract

A 2.7 kilobase pair (Kb) fragment of DNA, which complements mutations in the hisI locus of Escherichia coli, has been cloned and sequenced from the genome of the methanogenic archaebacterium Methanococcus vannielii. The cloned DNA directs the synthesis of three polypeptides, with molecular weights of 71,000, 29,000 and 15,600 in minicells of E. coli. Subcloning and mutagenesis demonstrates that hisI complementation results from the activity of the 15,600 molecular weight polypeptide. The primary structure of this archaebacterial gene and its gene product have been compared with the functionally equivalent gene and protein from the eubacterium E. coli (hisI) (Chiariotti et al. 1986) and from the eucaryote Saccharomyces cerevisiae (his4A) (Donahue et al. 1982). The DNA sequences of the archaebacterial and eubacterial genes are 40% homologous, the archaebacterial and eucaryotic DNA sequences are 47% homologous and, as previously reported (Bruni et al. 1986) the eubacterial and eucaryotic DNA sequences are 45% homologous. In E. coli the hisI locus is part of a bifunctional gene (hisI/E) within the single his operon. In S. cerevisiae the his4A locus is part of a multifunctional gene (his4) which encodes a protein with at least four enzymatic activities. The his genes of S. cerevisiae do not form an operon and are not physically linked. The M. vannielii hisI gene does not appear to be part of a multifunctional DNA sequence and, although it does appear to be within an operon, the open reading frames (ORFs) 5' and 3' to the M. vannielii hisI gene are not related to any published his sequences.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1986        PMID: 3018439     DOI: 10.1007/bf00330200

Source DB:  PubMed          Journal:  Mol Gen Genet        ISSN: 0026-8925


  28 in total

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Authors:  C R Woese; G E Fox
Journal:  Proc Natl Acad Sci U S A       Date:  1977-11       Impact factor: 11.205

Review 2.  Methanogens: reevaluation of a unique biological group.

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Journal:  Microbiol Rev       Date:  1979-06

3.  Genetic analysis of the histidine operon in Escherichia coli K12.

Authors:  E P Goldschmidt; M S Cater; T S Matney; M A Butler; A Greene
Journal:  Genetics       Date:  1970-10       Impact factor: 4.562

4.  Characterization of a halobacterial gene affecting bacterio-opsin gene expression.

Authors:  M Betlach; J Friedman; H W Boyer; F Pfeifer
Journal:  Nucleic Acids Res       Date:  1984-10-25       Impact factor: 16.971

5.  Cloning and expression of the distal portion of the histidine operon of Escherichia coli K-12.

Authors:  V Grisolia; M S Carlomagno; C B Bruni
Journal:  J Bacteriol       Date:  1982-08       Impact factor: 3.490

6.  Archaebacteria.

Authors:  C R Woese; L J Magrum; G E Fox
Journal:  J Mol Evol       Date:  1978-08-02       Impact factor: 2.395

7.  Characterization of the ribosomal RNA gene clusters in Halobacterium cutirubrum.

Authors:  I Hui; P P Dennis
Journal:  J Biol Chem       Date:  1985-01-25       Impact factor: 5.157

8.  The nucleotide sequence of the HIS4 region of yeast.

Authors:  T F Donahue; P J Farabaugh; G R Fink
Journal:  Gene       Date:  1982-04       Impact factor: 3.688

9.  Structure of genes and an insertion element in the methane producing archaebacterium Methanobrevibacter smithii.

Authors:  P T Hamilton; J N Reeve
Journal:  Mol Gen Genet       Date:  1985

10.  Non-repetitive AT-rich sequences are found in intergenic regions of Methanococcus voltae DNA.

Authors:  C Bollschweiler; R Kühn; A Klein
Journal:  EMBO J       Date:  1985-03       Impact factor: 11.598

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  17 in total

1.  An archaebacterial RNA polymerase binding site and transcription initiation of the hisA gene in Methanococcus vannielii.

Authors:  J W Brown; M Thomm; G S Beckler; G Frey; K O Stetter; J N Reeve
Journal:  Nucleic Acids Res       Date:  1988-01-11       Impact factor: 16.971

Review 2.  Histidine biosynthetic pathway and genes: structure, regulation, and evolution.

Authors:  P Alifano; R Fani; P Liò; A Lazcano; M Bazzicalupo; M S Carlomagno; C B Bruni
Journal:  Microbiol Rev       Date:  1996-03

Review 3.  Archaea and the prokaryote-to-eukaryote transition.

Authors:  J R Brown; W F Doolittle
Journal:  Microbiol Mol Biol Rev       Date:  1997-12       Impact factor: 11.056

Review 4.  The molecular genetics of C1 utilizing microorganisms. An overview.

Authors:  B W Holloway; P P Kearney; B R Lyon
Journal:  Antonie Van Leeuwenhoek       Date:  1987       Impact factor: 2.271

5.  Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii.

Authors:  C J Morris; J N Reeve
Journal:  J Bacteriol       Date:  1988-07       Impact factor: 3.490

6.  Molecular evolution of the histidine biosynthetic pathway.

Authors:  R Fani; P Liò; A Lazcano
Journal:  J Mol Evol       Date:  1995-12       Impact factor: 2.395

7.  The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis.

Authors:  Farah Javid-Majd; Dong Yang; Thomas R Ioerger; James C Sacchettini
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2008-05-14

8.  Catalytic zinc site and mechanism of the metalloenzyme PR-AMP cyclohydrolase.

Authors:  Robert L D'Ordine; Rebecca S Linger; Carolyn J Thai; V Jo Davisson
Journal:  Biochemistry       Date:  2012-07-09       Impact factor: 3.162

9.  Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae.

Authors:  M Kuenzler; T Balmelli; C M Egli; G Paravicini; G H Braus
Journal:  J Bacteriol       Date:  1993-09       Impact factor: 3.490

10.  Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.

Authors:  C Delorme; S D Ehrlich; P Renault
Journal:  J Bacteriol       Date:  1992-10       Impact factor: 3.490

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