The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues

Bork, Peer; Brown, Nigel P.; Hegyi, Hedvig; Schultz, Jörg

doi:10.1002/pro.5560050720

Cited by 187 publications

(226 citation statements)

References 31 publications

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“…Degenerate oligonucleotide primers (BJM1 and BJM2) were designed based on conserved PP2C sequences detected through the alignment of FEM-2 with other known and predicted PP2Cs. The annealing sites of these primers correspond to portions of PP2C motifs two and eight, of the 11 conserved motifs detected in a detailed sequence analysis of the PP2C superfamily (Bork et al 1996). To isolate PP2Cs from CB5161, PCR was performed using genomic DNA as the template.…”

Section: Methodsmentioning

confidence: 99%

“…XO m-z-Ce-fem-2(null) animals, either carrying a construct array or untransformed, were examined for somatic phenotype. At 20°C transgenic Ce-fem-2, Cb-fem-2, or Cs-fem-2 was able to rescue the somatic feminization in C. elegans fem-2 mutants, as were chimeric constructs consisting of the Ce-fem-2 promoter and UTRs fused to the Cb-fem-2 The PP2C motifs described by Bork et al (1996) are surrounded by gray boxes. B: Phylogenetic analysis of the sequence segments shown in the alignment.…”

Section: Transgenic Ce-fem-2 Cb-fem-2 or Cs-fem-2 Can Rescue Somatimentioning

confidence: 99%

“…In all three species FEM-2 contains a long amino terminal domain that is poorly conserved and absent from many other PP2Cs. There is also a group of acidic amino acids near the carboxy terminus that is not a general characteristic of PP2Cs (Bork et al 1996).…”

Section: Comparison Of Cs-fem-2 To Ce-fem-2 and Cb-fem-2mentioning

confidence: 99%

“…The PP2C motifs described by Bork et al (1996) are surrounded by gray boxes. Black circles mark the locations of the lesions associated with two temperature-sensitive alleles of Ce-fem-2, b245, and q117 (Pilgrim et al 1995), and functionally mutant forms of the Arabidopsis PP2Cs ABI1 and ABI2 (Leung et al 1994(Leung et al , 1997Meyer et al 1994).…”

Section: ) (F W Y) (K R H) (D E) (G a S) (P) (C) (T Nmentioning

confidence: 99%

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Evolution of the PP2C Family in Caenorhabditis: Rapid Divergence of the Sex-Determining Protein FEM-2

Stothard

Hansen²,

Pilgrim³

2002

J Mol Evol

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Abstract. To investigate the causes and functional significance of rapid sex-determining protein evolution we compared three Caenorhabditis elegans genes encoding members of the protein phosphatase 2C (PP2C) family with their orthologs from another Caenorhabditis species (strain CB5161). One of the genes encodes FEM-2, a sex-determining protein, while the others have no known sex-determining role. FEM-2's PP2C domain was found to be more diverged than the other PP2C domains, supporting the notion that sex-determining proteins are subjected to selective pressures that allow for or cause rapid divergence. Comparison of the positions of amino acid substitutions in FEM-2 with a solved three-dimensional structure suggests that the catalytic face of the protein is highly conserved among C. elegans, CB5161, and another closely related species C. briggsae. However, the non-conserved regions of FEM-2 cannot be said to lack functional importance, since fem-2 transgenes from the other species were unable to rescue the germ-line defect caused by a C. elegans fem-2 mutation. To test whether fem-2 functions as a sex-determining gene in the other Caenorhabditis species we used RNA-mediated interference (RNAi). fem-2 (RNAi) in C. elegans and C. briggsae caused germ-line feminization, but had no noticeable effect in CB5161. Thus the function of fem-2 in CB5161 remains uncertain.

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Section: Methodsmentioning

confidence: 99%

Section: Transgenic Ce-fem-2 Cb-fem-2 or Cs-fem-2 Can Rescue Somatimentioning

confidence: 99%

Section: Comparison Of Cs-fem-2 To Ce-fem-2 and Cb-fem-2mentioning

confidence: 99%

Section: ) (F W Y) (K R H) (D E) (G a S) (P) (C) (T Nmentioning

confidence: 99%

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Evolution of the PP2C Family in Caenorhabditis: Rapid Divergence of the Sex-Determining Protein FEM-2

Stothard

Hansen²,

Pilgrim³

2002

J Mol Evol

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“…The annealing sites of these primers correspond to portions of PP2C motifs two and eight, of the 11 conserved motifs detected in a detailed sequence analysis of the PP2C superfamily (Bork et al 1996). In an attempt to identify more distant PP2C orthologues, RNA from P. pacificus and Caenorhabditis species PS1010 was processed in the same manner, and C. briggsae RNA was used as a control to test the efficacy of the primers and methods used.…”

Section: Resultsmentioning

confidence: 99%

Conspecific and Interspecific Interactions Between the FEM-2 and the FEM-3 Sex-Determining Proteins Despite Rapid Sequence Divergence

Stothard

Pilgrim

2006

J Mol Evol

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Abstract. Using degenerate oligonucleotide primers, we isolated the Caenorhabditis remanei orthologue of the C. elegans sex-determining phosphatase gene fem-2 as well as two other protein phosphatase homologues. Despite the significant sequence divergence between C. elegans and C. remanei FEM-2, we used RNAi-mediated gene knockdown to demonstrate that at least some aspects of male development require FEM-2 function in C. remanei. Consistent with this functional conservation, the conspecific interaction between the FEM-2 and the FEM-3 proteins observed in C. elegans also occurs in C. remanei. To further explore whether the rapid evolution of FEM-2 and FEM-3 affects their molecular interactions, we tested for cross-species interactions between the proteins from C. elegans, C. briggsae, and C. remanei. Although all FEM-2/FEM-3 pairs from a single species interact, only two out of six interspecific pairs bind each other, showing that FEM-2 and FEM-3 are coevolving. Both interspecific interactions involved C. briggsae FEM-3. We constructed chimeric versions of FEM-2 consisting of various combinations of the C. elegans and C. remanei proteins. C. briggsae FEM-3 interacted with all the chimeras, even those that did not interact with either C. elegans or C. remanei FEM-3. We hypothesize that the promiscuity of C. briggsae FEM-3 reflects an increased reliance on evolutionarily constrained regions of FEM-2 for binding. If so, our data support the notion that the coevolution of two interacting proteins sometimes involves a shift in the domains that contribute to binding.

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Serine/Threonine Kinases and Phosphatases

Girault

2002

Encyclopedia of Molecular Biology

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The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues

Cited by 187 publications

References 31 publications

Evolution of the PP2C Family in Caenorhabditis: Rapid Divergence of the Sex-Determining Protein FEM-2

Evolution of the PP2C Family in Caenorhabditis: Rapid Divergence of the Sex-Determining Protein FEM-2

Conspecific and Interspecific Interactions Between the FEM-2 and the FEM-3 Sex-Determining Proteins Despite Rapid Sequence Divergence

Serine/Threonine Kinases and Phosphatases

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