Biochemical evidence that <i>Saccharomyces cerevisiae YGR262c</i> gene, required for normal growth, encodes a novel Ser/Thr‐specific protein kinase

Stocchetto, S.; Marin, Oriano; Carignani, Giovanna; Pinna, Lorenzo A.

doi:10.1016/s0014-5793(97)00980-0

Cited by 36 publications

(60 citation statements)

References 24 publications

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“…Experimental evidence shows that it is a Ser/ Thr-specific kinase required for normal growth of the yeast (Stocchetto et al 1997). Interestingly, this kinase displays some unique features when compared to conventional ePKs; including resistance to staurosporine and a requirement for Mn 2+ instead of Mg 2+ (Stocchetto et al 1997). …”

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confidence: 99%

Novel Families of Putative Protein Kinases in Bacteria and Archaea: Evolution of the “Eukaryotic” Protein Kinase Superfamily

Leonard¹,

Aravind²,

Koonin³

1998

Genome Res.

293

285

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The central role of serine/threonine and tyrosine protein kinases in signal transduction and cellular regulation in eukaryotes is well established and widely documented. Considerably less is known about the prevalence and role of these protein kinases in bacteria and archaea. In order to examine the evolutionary origins of the eukaryotic-type protein kinase (ePK) superfamily, we conducted an extensive analysis of the proteins encoded by the completely sequenced bacterial and archaeal genomes. We detected five distinct families of known and predicted putative protein kinases with representatives in bacteria and archaea that share a common ancestry with the eukaryotic protein kinases. Four of these protein families have not been identified previously as protein kinases. From the phylogenetic distribution of these families, we infer the existence of an ancestral protein kinase(s) prior to the divergence of eukaryotes, bacteria, and archaea.For many years after the discovery of protein phosphorylation, the prevailing view was that phosphorylation of proteins on serine, threonine, and tyrosine residues was a phenomenon restricted to the eukaryotes, in which these modifications perform important regulatory functions (Hanks et al. 1988;Hunter 1995). In bacteria, an analogous regulatory role was attributed to the two-component sensor kinases and the phosphoenolpyruvatedependent phosphotransferase systems, which typically catalyze the phosphorylation of proteins on histidine and aspartate residues, respectively (Saier et al. 1990). Further experimental work has brought to light exceptions to these paradigms. Evidence of bacterial Koshland 1978, 1981) and archaeal (Skorko 1984; proteins containing phosphoserine, phosphothreonine, or phosphotyrosine residues has accumulated over the past two decades, and elements of the twocomponent sensor kinase system have been detected in archaea and eukaryotes (Loomis et al. 1997).Several unusual mechanisms of Ser/Thr or Tyr protein phosphorylation have been recognized in prokaryotes, but they do not appear universally in bacteria or archaebacteria. There are examples of histidine kinase-related proteins in Bacillus subtilis (Yang et al. 1996) and the eukaryotic mitochondrion (Popov et al. 1992) that mediate phosphoserine formation. In addition, there have been reports of Ser/Thr or Tyr autophosphorylating proteins in bacteria (Ostrovsky and Maloy 1995;Grangeasse et al. 1997).Recently, genes encoding proteins homologous to eukaryotic Ser/Thr protein kinases have been identified in several bacteria (Kennelly and Potts 1996) and archaea (Smith and King 1995). Myxococcus xanthus encodes numerous paralogous Ser/Thr kinases that show highly significant sequence similarity to one another (Munoz-Dorado et al. 1993). The best characterized of these proteins, Pkn2, has been shown to play a regulatory role in secretion (Udo et al. 1995). Protein kinases of the Pkn2 type have also been recognized in a number of other bacteria (Zhang 1996).To evaluate the entire repertoire of potential protein k...

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confidence: 99%

Novel Families of Putative Protein Kinases in Bacteria and Archaea: Evolution of the “Eukaryotic” Protein Kinase Superfamily

Leonard¹,

Aravind²,

Koonin³

1998

Genome Res.

293

285

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“…Interestingly, not only did full-size bPrP stimulate calmodulin phosphorylation by CK2α (compare the first and third lanes of Figure 3A), it also abolished the negative effect of β subunits present in the reconstituted holoenzyme (compare the second and fourth lanes of Figure 3A). In contrast, the catalytic activity of three other acidophilic protein kinases, two Ser\Thr-specific (CK1 and piD261 [13]) and one Tyr-specific (Syk), were unaffected by bPrP under the conditions used (results not shown).…”

Section: Figure 2 Detection Of the Interaction Of Ck2 And Full-size Bmentioning

confidence: 89%

“…Casein kinase 1 (CK1) was either obtained as a recombinant Xenopus lae is isoform (CK1α) [12] or purified from rat liver cytosol as described previously [10]. Recombinant piD261 protein kinase was prepared as described [13]. Tyrosine protein kinase Syk, purified from bovine spleen, was kindly provided by Dr A. M. Brunati (Padova, Italy).…”

Section: Experimental Materialsmentioning

confidence: 99%

Bovine prion protein as a modulator of protein kinase CK2

Meggio

Negro

Sarno

et al. 2000

Biochemical Journal

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On the basis of far-Western blot and plasmon resonance (BIAcore) experiments, we show here that recombinant bovine prion protein (bPrP) (25-242) strongly interacts with the catalytic α\αh subunits of protein kinase CK2 (also termed ' casein kinase 2 '). This association leads to increased phosphotransferase activity of CK2α, tested on calmodulin or specific peptides as substrate. We also show that bPrP counteracts the inhibition of calmodulin phosphorylation promoted by the regulatory β subunits of CK2. A truncated form of bPrP encompassing the Cterminal domain (residues 105-242) interacts with CK2 but does

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“…EKC/KEOPS complex is required for bipolar bud-site selection BUD32 was originally found as a gene encoding an atypical protein kinase found in virtually all eukaryotic and archaeal organisms (Stocchetto et al 1997). It was also identified as a gene that regulates bud-site selection of diploid cells through a genome-wide analysis (Ni and Snyder 2001).…”

Section: Discussionmentioning

confidence: 99%

“…The homozygous deletion mutant of the gene BUD32 displayed a random budding pattern (Ni and Snyder 2001). BUD32 was originally found as a gene encoding an atypical protein kinase that belongs to the piD261 family of atypical Ser/Thr protein kinases found in virtually all eukaryotic and archaeal organisms (Stocchetto et al 1997). Recently, two independent studies of haploid cells have shown that Bud32p is a component of the KEOPS (kinase, putative endopeptidase, and other proteins of small size) or the EKC (endopeptidase-like, kinase, chromatinassociated) complexes with functions of telomere maintenance and transcriptional regulation, respectively (Downey et al 2006;Kisseleva-Romanova et al 2006).…”

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confidence: 99%

Cell Polarity in Saccharomyces cerevisiae Depends on Proper Localization of the Bud9 Landmark Protein by the EKC/KEOPS Complex

et al. 2011

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In diploid Saccharomyces cerevisiae cells, bud-site selection is determined by two cortical landmarks, Bud8p and Bud9p, at the distal and proximal poles, respectively. Their localizations depend on the multigenerational proteins Rax1p/Rax2p. Many genes involved in bud-site selection were identified previously by genome-wide screening of deletion mutants, which identified BUD32 that causes a random budding in diploid cells. Bud32p is an atypical kinase involved in a signaling cascade of Sch9p kinase, the yeast homolog of Akt/PKB, and a component of the EKC/KEOPS (endopeptidase-like, kinase, chromatin-associated/kinase, putative endopeptidase, and other proteins of small size) complex that functions in telomere maintenance and transcriptional regulation. However, its role in bipolar budding has remained unclear. In this report, we show that the Sch9p kinase cascade does not affect bipolar budding but that the EKC/KEOPS complex regulates the localization of Bud9p. The kinase activity of Bud32p, which is essential for the functions of the EKC/KEOPS complex but is not necessary for the Sch9p signaling cascade, is required for bipolar bud-site selection. BUD9 is necessary for random budding in each deletion mutant of EKC/KEOPS components, and RAX2 is genetically upstream of EKC/KEOPS genes for the regulation of bipolar budding. The asymmetric localization of Bud9p was dependent on the complex, but Bud8p and Rax2p were not. We concluded that the EKC/KEOPS complex is specifically involved in the regulation of Bud9p localization downstream of Rax1p/Rax2p.

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Biochemical evidence that Saccharomyces cerevisiae YGR262c gene, required for normal growth, encodes a novel Ser/Thr‐specific protein kinase

Cited by 36 publications

References 24 publications

Novel Families of Putative Protein Kinases in Bacteria and Archaea: Evolution of the “Eukaryotic” Protein Kinase Superfamily

Novel Families of Putative Protein Kinases in Bacteria and Archaea: Evolution of the “Eukaryotic” Protein Kinase Superfamily

Bovine prion protein as a modulator of protein kinase CK2

Cell Polarity in Saccharomyces cerevisiae Depends on Proper Localization of the Bud9 Landmark Protein by the EKC/KEOPS Complex

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