Literature DB >> 2251731

Regulation of bacterial physiological processes by three types of protein phosphorylating systems.

M H Saier1, L F Wu, J Reizer.   

Abstract

A single type of protein-phosphorylating system, the ATP-dependent protein kinases, is employed in the regulation of a variety of cellular physiological processes in eukaryotes. By contrast, recent work with bacteria has revealed that three types of protein-phosphorylating systems are involved in regulation: (1) the classical protein kinases, (2) the newly discovered sensor-kinase/response-regulator systems, and (3) the multifaceted phosphoenolpyruvate-dependent phosphotransferase system. Physiological and mechanistic aspects of these three evolutionarily distinct systems are discussed.

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Year:  1990        PMID: 2251731     DOI: 10.1016/0968-0004(90)90238-7

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  19 in total

1.  Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis.

Authors:  C Mitchell; P W Morris; J C Vary
Journal:  J Bacteriol       Date:  1992-04       Impact factor: 3.490

Review 2.  Diversity and specificity of protein-phosphorylating systems in bacteria.

Authors:  A J Cozzone
Journal:  Folia Microbiol (Praha)       Date:  1997       Impact factor: 2.099

3.  Hexokinase as a sugar sensor in higher plants.

Authors:  J C Jang; P León; L Zhou; J Sheen
Journal:  Plant Cell       Date:  1997-01       Impact factor: 11.277

4.  Characterization of ornithine decarboxylase and regulation by its antizyme in Thermus thermophilus.

Authors:  A A Pantazaki; C G Anagnostopoulos; E E Lioliou; D A Kyriakidis
Journal:  Mol Cell Biochem       Date:  1999-05       Impact factor: 3.396

5.  Osmoregulation of the fatty acid receptor gene fadL in Escherichia coli.

Authors:  A Higashitani; Y Nishimura; H Hara; H Aiba; T Mizuno; K Horiuchi
Journal:  Mol Gen Genet       Date:  1993-09

6.  Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system.

Authors:  J Deutscher; B Bauer; H Sauerwald
Journal:  J Bacteriol       Date:  1993-06       Impact factor: 3.490

7.  Purification of Potato Leaf Plasma Membrane Protein pp34, a Protein Phosphorylated in Response to Oligogalacturonide Signals for Defense and Development.

Authors:  T. Jacinto; E. E. Farmer; C. A. Ryan
Journal:  Plant Physiol       Date:  1993-12       Impact factor: 8.340

8.  Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution.

Authors:  G M Pao; M H Saier
Journal:  J Mol Evol       Date:  1995-02       Impact factor: 2.395

9.  Cloning and expression of a new human polypeptide which regulates protein phosphorylation in Escherichia coli.

Authors:  A Daniele; F Altruda; M Ferrone; L Silengo; L Chiarantini; M Bianchi; V Stocchi; M Magnani
Journal:  Mol Cell Biochem       Date:  1991-10-16       Impact factor: 3.396

10.  Expression of hydrogenase in Hupc strains of Bradyrhizobium japonicum.

Authors:  H Kim; C Gabel; R J Maier
Journal:  Arch Microbiol       Date:  1993       Impact factor: 2.552

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