title: Myxococcus xanthus Pph2 is a manganese-dependent protein phosphatase involved in energy metabolism.
abstract: The multicellular behavior of the myxobacterium Myxococcus xanthus requires the participation of an elevated number of signal-transduction mechanisms to coordinate the cell movements and the sequential changes in gene expression patterns that lead to the morphogenetic and differentiation events. These signal-transduction mechanisms are mainly based on two-component systems and on the reversible phosphorylation of protein targets mediated by eukaryotic-like protein kinases and phosphatases. Among all these factors, protein phosphatases are the elements that remain less characterized. Hence, we have studied in this work the physiological role and biochemical activity of the protein phosphatase of the family PPP (phosphoprotein phosphatases) designated as Pph2, which is forming part of the same operon as the two-component system phoPR1. We have demonstrated that this operon is induced upon starvation in response to the depletion of the cell energy levels. The increase in the expression of the operon contributes to an efficient use of the scarce energy resources available for developing cells to ensure the completion of the life cycle. In fact, a Deltapph2 mutant is defective in aggregation, sporulation yield, morphology of the myxospores, and germination efficiency. The yeast two-hybrid technology has shown that Pph2 interacts with the gene products of MXAN_1875 and 5630, which encode a hypothetical protein and a glutamine synthetase, respectively. Because Pph2 exhibits Ser/Thr, and to some extent Tyr, Mn(2+)-dependent protein phosphatase activity, it is expected that this function is accomplished by dephosphorylation of the specific protein substrates.
authors.affiliation: Departamento de Microbiología, Facultad de Ciencias, Universidad de Granada, E-18071 Granada, Spain.
authors.forename: Raquel
authors.initials: R
authors.lastname: García-Hernández
authors.forename: Aurelio
authors.initials: A
authors.lastname: Moraleda-Muñoz
authors.forename: Alfredo
authors.initials: A
authors.lastname: Castañeda-García
authors.forename: Juana
authors.initials: J
authors.lastname: Pérez
authors.forename: José
authors.initials: J
authors.lastname: Muñoz-Dorado
mesh_terms: D004734:Energy Metabolism; D004926:Escherichia coli / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D005800:Genes, Fungal; D016680:Genome, Bacterial; D005974:Glutamate-Ammonia Ligase / Q000737:chemistry; D007763:Lac Operon; D008345:Manganese / Q000737:chemistry*; D016941:Myxococcus xanthus / Q000378:metabolism*; D009841:Oligonucleotides / Q000737:chemistry; D010641:Phenotype; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D010766:Phosphorylation; D020798:Two-Hybrid System Techniques
chemical_list: D009841:Oligonucleotides; D008345:Manganese; D010749:Phosphoprotein Phosphatases; D005974:Glutamate-Ammonia Ligase
references.citation: J Bacteriol. 2003 Feb;185(4):1376-83
references.pmid: 12562808
references.citation: J Biol Chem. 1994 Oct 21;269(42):26234-8
references.pmid: 7929339
references.citation: Gene. 1985;33(1):103-19
references.pmid: 2985470
references.citation: Appl Environ Microbiol. 2002 May;68(5):2368-75
references.pmid: 11976110
references.citation: Biochem J. 2002 Sep 15;366(Pt 3):929-36
references.pmid: 12059787
references.citation: J Bacteriol. 2005 Jul;187(14):4976-83
references.pmid: 15995213
references.citation: Curr Genet. 1989 Dec;16(5-6):339-46
references.pmid: 2692852
references.citation: J Bacteriol. 1979 Dec;140(3):1036-42
references.pmid: 118153
references.citation: Science. 1995 Oct 27;270(5236):641-4
references.pmid: 7570023
references.citation: Mol Cell Proteomics. 2007 Apr;6(4):697-707
references.pmid: 17218307
references.citation: Mol Microbiol. 1999 Oct;34(2):268-81
references.pmid: 10564471
references.citation: Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):9098-103
references.pmid: 10922065
references.citation: Microbiology (Reading). 2004 Dec;150(Pt 12):4189-4197
references.pmid: 15583171
references.citation: J Bacteriol. 2008 Mar;190(6):1997-2003
references.pmid: 18178740
references.citation: J Bacteriol. 1998 Aug;180(16):4030-5
references.pmid: 9696747
references.citation: EMBO J. 1997 Apr 1;16(7):1670-85
references.pmid: 9130712
references.citation: Microbiol Mol Biol Rev. 1999 Jun;63(2):479-506
references.pmid: 10357859
references.citation: Annu Rev Microbiol. 1983;37:551-73
references.pmid: 6314878
references.citation: Nucleic Acids Res. 1992 Jul 25;20(14):3790
references.pmid: 1641351
references.citation: J Bacteriol. 2001 Dec;183(24):7053-7
references.pmid: 11717262
references.citation: Gene. 2000 Nov 27;258(1-2):55-62
references.pmid: 11111042
references.citation: Mol Microbiol. 2001 Apr;40(1):126-40
references.pmid: 11298281
references.citation: J Bacteriol. 1998 May;180(10):2616-22
references.pmid: 9573144
references.citation: Arch Microbiol. 2004 Mar;181(3):171-81
references.pmid: 14745484
references.citation: Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15950-5
references.pmid: 18836084
references.citation: Eur J Biochem. 1994 Feb 15;220(1):225-37
references.pmid: 8119291
references.citation: Mol Microbiol. 1995 Feb;15(3):483-94
references.pmid: 7783619
references.citation: Genetics. 1996 Dec;144(4):1425-36
references.pmid: 8978031
references.citation: Mol Microbiol. 2003 Jul;49(2):517-28
references.pmid: 12828646
references.citation: J Bacteriol. 1990 May;172(5):2294-302
references.pmid: 2158968
references.citation: Mol Microbiol. 2002 Dec;46(5):1353-66
references.pmid: 12453221
references.citation: Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15200-5
references.pmid: 17015832
references.citation: FEMS Microbiol Rev. 1998 Oct;22(4):229-53
references.pmid: 9862122
references.citation: Biochemistry. 2000 Dec 19;39(50):15365-74
references.pmid: 11112522
references.citation: Mol Cell Proteomics. 2008 Feb;7(2):299-307
references.pmid: 17938405
references.citation: Antonie Van Leeuwenhoek. 2003;83(4):361-8
references.pmid: 12777072
references.citation: Chem Rev. 2001 Aug;101(8):2313-40
references.pmid: 11749375
references.citation: Methods Enzymol. 1991;201:389-98
references.pmid: 1658556
references.citation: J Bacteriol. 2006 Mar;188(6):2154-62
references.pmid: 16513745
references.citation: Mol Microbiol. 2000 Jan;35(1):180-8
references.pmid: 10632888
references.citation: Nat Biotechnol. 2007 Nov;25(11):1281-9
references.pmid: 17965706