Protein Phosphatases−A Phylogenetic Perspective

Kennelly, Peter J.

doi:10.1021/cr0002543

Cited by 73 publications

(65 citation statements)

References 284 publications

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Section: Archaeal Protein Kinases and Phosphatasesmentioning

confidence: 99%

“…In contrast, protein kinases and phosphatases, the enzymes responsible for the addition and removal, respectively, of orthophosphate groups from target proteins, contain conserved sequence motifs (213). Based on such motifs, protein kinases and phosphatases can be divided into several functional families (213). Thus, the availability of several archaeal genome sequences has allowed a catalogue of the potential protein kinases and phosphatases to be assembled (214,215).…”

Section: Archaeal Protein Kinases and Phosphatasesmentioning

confidence: 99%

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Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Archaeal Protein Kinases and Phosphatasesmentioning

confidence: 99%

Section: Archaeal Protein Kinases and Phosphatasesmentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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“…Genes encoding serine/threonine-type protein phosphatase (PP) have been found in all three domains of life, Archaea, Bacteria and Eukarya (Kennelly, 2001 (Bork et al, 1996). Among the genomes searched, the two Streptomyces species we studied previously contained the largest numbers of PPMs (49 PPMs for S. coelicolor, and 48 PPMs for S. avermitilis), followed by Synechocystis sp.…”

Section: Identification Of Ppm Proteinsmentioning

confidence: 99%

Evolution of the PPM-family protein phosphatases in Streptomyces: duplication of catalytic domain and lateral recruitment of additional sensory domains

Zhang

Shi

2004

Microbiology

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Originally identified from eukaryotes, the Mg 2+ -or Mn 2+ -dependent protein phosphatases (PPMs) are a diverse group of enzymes whose members include eukaryotic PP2C and some prokaryotic serine/threonine phosphatases. In a previous study, unexpectedly large numbers of PPMs were identified in two Streptomyces genomes. In this work, a phylogenetic analysis was performed with all the PPMs available from a wide variety of microbial sources to determine the evolutionary origin of the Streptomyces PPM proteins. Consistent with earlier hypotheses, the results suggested that the microbial PPMs were relatively recent additions from eukaryotic sources. Results also indicated that the Streptomyces PPMs were divided into two major subfamilies at an early stage of their emergence in Streptomyces genomes. The first subfamily, which contains only six Streptomyces PPMs, possesses a catalytic domain whose sequence and architecture are similar to that of eukaryotic PPMs; the second subfamily contains 89 Streptomyces PPMs that lack the 5a and 5b catalytic domain motifs, similar to the PPMs SpoIIE and RsbU of Bacillus subtilis. Significant gene duplication was observed for the PPMs in the second subfamily. In addition, more than half (54 %) of the Streptomyces PPMs from the second subfamily were found to have at least one additional sensory domain, most commonly the PAS or the GAF domain. Phylogenetic analysis showed that these domains tended to be clustered according to the putative physiological functions rather than taxonomic relationship, implying that they might have arisen as a result of domain recruitment in a late evolutionary stage. This study provides an insight into how Streptomyces spp. may have expanded their PPM-based signal transduction networks to enable them to respond to a greater range of environmental changes.

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“…The Protein Phosphatase Database (http://www.phosphatase.biochem.vt.edu) organizes information retrieved from the primary scientific literature, focusing on and limiting its effort to prokaryotic phosphatases [8]. PhosphaBase is a database that organizes phosphatase sequence information retrieved from UniprotKB [9].…”

Section: Introductionmentioning

confidence: 99%

HUPHO: the human phosphatase portal

et al. 2012

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Phosphatases and kinases contribute to the regulation of protein phosphorylation homeostasis in the cell. Phosphorylation is a key post-translational modification underlying the regulation of many cellular processes. Thus, a comprehensive picture of phosphatase function and the identification of their target substrates would aid a systematic approach to a mechanistic description of cell signalling. Here we present a website designed to facilitate the retrieval of information about human protein phosphatases. To this end we developed a search engine to recover and integrate information annotated in several publicly available web resources. In addition we present a text-mining-assisted annotation effort aimed at extracting phosphatase related data reported in the scientific literature. The HuPho (human phosphatases) website can be accessed at http://hupho.uniroma2.it.

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Protein Phosphatases−A Phylogenetic Perspective

Cited by 73 publications

References 284 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Evolution of the PPM-family protein phosphatases in Streptomyces: duplication of catalytic domain and lateral recruitment of additional sensory domains

HUPHO: the human phosphatase portal

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