RdgC/PP5-Related Phosphatases

Андреева, А. В.; Kutuzov, Mikhail A.

doi:10.1016/s0898-6568(99)00032-7

Cited by 43 publications

(8 citation statements)

References 57 publications

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“…At their C-termini, the kinetoplastid PPEFs are more closely related to the C-termini of the RdgC/PPEFs than to any other calcium binding proteins or EF-hand domain-containing enzymes [35]. This observation supports the hypothesis that the catalytic domain of the ancestral form of RdgcC/PPEF fused with an EF-hand Ca 2+ -binding protein prior to the acquisition of the N-terminal domain [1].…”

Section: Resultssupporting

confidence: 72%

Kinetoplastid PPEF phosphatases: Dual acylated proteins expressed in the endomembrane system of Leishmania

Mills

Price

Johner

et al. 2007

Molecular and Biochemical Parasitology

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Bioinformatic analyses have been used to identify potential downstream targets of the essential enzyme N-myristoyl transferase in the TriTryp species, Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. These database searches predict ∼60 putative N-myristoylated proteins with high confidence, including both previously characterised and novel molecules. One of the latter is an N-myristoylated protein phosphatase which has high sequence similarity to the Protein Phosphatase with EF-Hand (PPEF) proteins identified in sensory cells of higher eukaryotes. In L. major and T. brucei, the PPEF-like phosphatases are encoded by single-copy genes and are constitutively expressed in all parasite life cycle stages. The N-terminus of LmPPEF is a substrate for N-myristoyl transferase and is also palmitoylated in vivo. The wild type protein has been localised to the endocytic system by immunofluorescence. The catalytic and fused C-terminal domains of the kinetoplastid and other eukaryotic PPEFs share high sequence similarity, but unlike their higher eukaryotic relatives, the C-terminal parasite EF-hand domains are degenerate and do not bind calcium.

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Section: Resultssupporting

confidence: 72%

Kinetoplastid PPEF phosphatases: Dual acylated proteins expressed in the endomembrane system of Leishmania

Mills

Price

Johner

et al. 2007

Molecular and Biochemical Parasitology

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“…In some cases, such as PP5 (reviewed in ref 74), these auxiliary domains are fused directly onto the catalytic polypeptide chain. However, in most cases these auxiliary domains are incorporated in the form of dissociable subunits.…”

Section: Eukaryotic Pppsmentioning

confidence: 99%

Protein Phosphatases−A Phylogenetic Perspective

Kennelly

2001

Chem. Rev.

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“…Reversible protein phosphorylation mediated by protein kinases and protein phosphatases is a major event in signal transduction, regulating many biological processes including cell cycle events, growth factor response, hormone and other environmental stimuli, metabolic control and developmental events [1-6]. During phosphorylation, a protein kinase adds a phosphate group to a substrate.…”

Section: Introductionmentioning

confidence: 99%

Protein phosphatase complement in rice: genome-wide identification and transcriptional analysis under abiotic stress conditions and reproductive development

et al. 2010

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BackgroundProtein phosphatases are the key components of a number of signaling pathways where they modulate various cellular responses. In plants, protein phosphatases constitute a large gene family and are reportedly involved in the regulation of abiotic stress responses and plant development. Recently, the whole complement of protein phosphatases has been identified in Arabidopsis genome. While PP2C class of serine/threonine phosphatases has been explored in rice, the whole complement of this gene family is yet to be reported.ResultsIn silico investigation revealed the presence of 132-protein phosphatase-coding genes in rice genome. Domain analysis and phylogenetic studies of evolutionary relationship categorized these genes into PP2A, PP2C, PTP, DSP and LMWP classes. PP2C class represents a major proportion of this gene family with 90 members. Chromosomal localization revealed their distribution on all the 12 chromosomes, with 42 genes being present on segmentally duplicated regions and 10 genes on tandemly duplicated regions of chromosomes. The expression profiles of 128 genes under salinity, cold and drought stress conditions, 11 reproductive developmental (panicle and seed) stages along with three stages of vegetative development were analyzed using microarray expression data. 46 genes were found to be differentially expressing in 3 abiotic stresses out of which 31 were up-regulated and 15 exhibited down-regulation. A total of 82 genes were found to be differentially expressing in different developmental stages. An overlapping expression pattern was found for abiotic stresses and reproductive development, wherein 8 genes were up-regulated and 7 down-regulated. Expression pattern of the 13 selected genes was validated employing real time PCR, and it was found to be in accordance with the microarray expression data for most of the genes.ConclusionsExploration of protein phosphatase gene family in rice has resulted in the identification of 132 members, which can be further divided into different classes phylogenetically. Expression profiling and analysis indicate the involvement of this large gene family in a number of signaling pathways triggered by abiotic stresses and their possible role in plant development. Our study will provide the platform from where; the expression pattern information can be transformed into molecular, cellular and biochemical characterization of members belonging to this gene family.

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RdgC/PP5-Related Phosphatases

Cited by 43 publications

References 57 publications

Kinetoplastid PPEF phosphatases: Dual acylated proteins expressed in the endomembrane system of Leishmania

Kinetoplastid PPEF phosphatases: Dual acylated proteins expressed in the endomembrane system of Leishmania

Protein Phosphatases−A Phylogenetic Perspective

Protein phosphatase complement in rice: genome-wide identification and transcriptional analysis under abiotic stress conditions and reproductive development

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