Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation.

Udo, Hiroshi; Muñoz‐Dorado, José; Inouye, Masayori; Inouye, Sumiko

doi:10.1101/gad.9.8.972

Cited by 57 publications

(75 citation statements)

References 39 publications

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“…A similar result was found with an 18-residue hydrophobic stretch in Pkn2 (Udo et al, 1995). Because PhoA is known to be active only when it is translocated across the membrane (Manoil and Beckwith, 1985), these data demonstrate that the 22 hydrophobic residues of Pkn9 function as an internal signal sequence, translocating the downstream residues across the membrane.…”

Section: Pkn9 Contains a Transmembrane Domainsupporting

confidence: 80%

“…In order to demonstrate that the 22 hydrophobic amino acid residues (residues 401-422) of the deduced Pkn9 sequence can serve as a transmembrane domain, internal signal-sequence fusion proteins of Pkn9 and Escherichia coli alkaline phosphatase (PhoA) were constructed with and without the putative transmembrane domain, as previously described for Pkn2 (Udo et al, 1995) (Fig. 4).…”

Section: Pkn9 Contains a Transmembrane Domainmentioning

confidence: 99%

“…Additional work indicated that a large family of eukaryotic-like Ser/ Thr protein kinases exist in M. xanthus (Zhang et al, 1992), suggesting that there are multiple signalling cascades consisting of Ser/Thr protein kinases that allow M. xanthus to respond to environmental changes. The mostrecent studies indicate that a transmembrane-anchored eukaryotic-like Ser/Thr kinase, Pkn2, regulates the activity of endogenous ␤-lactamase or related enzymes in response to environmental signals (Udo et al, 1995), and that two other kinases, Pkn5 and Pkn6, also play important roles in the fruiting-body formation (Zhang et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

“…This region is likely to serve as a stop transfer signal for the insertion of this protein into the membrane (Kim et al, 1994). Recently, Pkn2 was reported to contain a similar transmembrane domain (Udo et al, 1995). Just downstream of the putative transmembrane domain there are tandem repeats of 13 amino acid residues: PQQAAAPEQtAAV (residues 437-449) and PQQAAAPEQaAAV (residues 451-463); separated by a threonine residue at position 450.…”

Section: Introductionmentioning

confidence: 99%

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Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus

Hanlon

Inouye

1997

Molecular Microbiology

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SummaryThe Myxococcus xanthus gene, pkn9, encodes a protein that contains significant homology with eukaryotic Ser/ Thr protein kinases. The pkn9 gene was singled out of a previously identified family of kinase genes by amplification techniques that displayed differences in kinase gene expression during selected periods of the M. xanthus life cycle. Pkn9 was constitutively expressed during vegetative growth and upregulated during the aggregation stage of early development. It consists of 589 amino acids, and its N-terminal 394 residues show 38% identity with both Pkn1 and Pkn2 of M. xanthus. This region also shows 29, 25 and 29% identity with myosin light-chain kinase, protein kinase C, and cAMP-dependent protein kinase, respectively. A 22-residue hydrophobic transmembrane domain separates the kinase domain from the 173-residue C-terminal domain that resides on the outside of the inner membrane. The C-terminal domain contains two sets of tandem repeats of 13 and 10 residues which have no known function. When expressed in Escherichia coli under the T7 promoter, Pkn9 was found to be phosphorylated on serine and threonine residues. Disruption of the pkn9 kinase catalytic subdomains I-III by the insertion of a kanamycin-resistance gene resulted in slightly delayed, smaller and more-crowded fruiting bodies, while spore formation was normal. Total deletion of the pkn9 gene caused severely reduced progression through development resulting in light loose mounds that become slightly more compact over time. Development progressed further at the centre than at the edge of the spot, and spore formation was significantly reduced. Twodimensional gel analysis revealed that both the disruption and the deletion of pkn9 prevented the expression of five membrane proteins (KREP9-1-4). These results suggest that the loss of Pkn9 kinase activity caused altered fruiting-body formation, the absence of the KREP9 proteins in the membrane, and reduced spore production.

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Section: Pkn9 Contains a Transmembrane Domainsupporting

confidence: 80%

Section: Pkn9 Contains a Transmembrane Domainmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus

Hanlon

Inouye

1997

Molecular Microbiology

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“…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).…”

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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.

298

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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The Molecular Biology of Plant Hormone Reception

Bassett

2000

Horticultural Reviews

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Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation.

Cited by 57 publications

References 39 publications

Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus

Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus

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

The Molecular Biology of Plant Hormone Reception

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