scholarly journals Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility ofSulfolobus acidocaldarius

2016 ◽  
Vol 6 (1) ◽  
pp. e00414 ◽  
Author(s):  
Lena Hoffmann ◽  
Andreas Schummer ◽  
Julia Reimann ◽  
Maria F. Haurat ◽  
Amanda J. Wilson ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Regulatory Network ◽  
Eukaryotic Protein ◽  
Eukaryotic Protein Kinases

scholarly journals Open Reading Frame sso2387 from the Archaeon Sulfolobus solfataricus Encodes a Polypeptide with Protein-Serine Kinase Activity

2003 ◽  
Vol 185 (11) ◽  
pp. 3436-3445 ◽  
Author(s):  
Brian H. Lower ◽  
Peter J. Kennelly
Keyword(s):  
Protein Kinases ◽  
Catalytic Domain ◽  
Sulfolobus Solfataricus ◽  
Open Reading Frame ◽  
Serine Kinase ◽  
Eukaryotic Protein Kinase ◽  
Reading Frame ◽  
Eukaryotic Protein ◽  
High Concentrations ◽  
Eukaryotic Protein Kinases

ABSTRACT The predicted polypeptide product of open reading frame sso2387 from the archaeon Sulfolobus solfataricus, SsoPK2, displayed several of the sequence features conserved among the members of the “eukaryotic” protein kinase superfamily. sso2387 was cloned, and its polypeptide product was expressed in Escherichia coli. The recombinant protein, rSsoPK2, was recovered in insoluble aggregates that could be dispersed by using high concentrations (5 M) of urea. The solubilized polypeptide displayed the ability to phosphorylate itself as well as several exogenous proteins, including mixed histones, casein, bovine serum albumin, and reduced carboxyamidomethylated and maleylated lysozyme, on serine residues. The source of this activity resided in that portion of the protein displaying homology to the catalytic domain of eukaryotic protein kinases. By use of mass spectrometry, the sites of autophosphorylation were found to be located in two areas, one immediately N terminal to the region corresponding to subdomain I of eukaryotic protein kinases, and the second N terminal to the presumed activation loop located between subdomains VII and VIII. Autophosphorylation of rSsoPK2 could be uncoupled from the phosphorylation of exogenous proteins by manipulation of the temperature or mutagenic alteration of the enzyme. Autophosphorylation was detected only at temperatures ≥60°C, whereas phosphorylation of exogenous proteins was detectable at 37°C. Similarly, replacement of one of the potential sites of autophosphorylation, Ser548, with alanine blocked autophosphorylation but not phosphorylation of an exogenous protein, casein.

scholarly journals The Landscape of Atypical and Eukaryotic Protein Kinases

2019 ◽  
Vol 40 (11) ◽  
pp. 818-832 ◽  
Author(s):  
Georgi K. Kanev ◽  
Chris de Graaf ◽  
Iwan J.P. de Esch ◽  
Rob Leurs ◽  
Thomas Würdinger ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Eukaryotic Protein ◽  
Eukaryotic Protein Kinases

scholarly journals An evolutionary perspective on the kinome of malaria parasites

2012 ◽  
Vol 367 (1602) ◽  
pp. 2607-2618 ◽  
Author(s):  
Eric Talevich ◽  
Andrew B. Tobin ◽  
Natarajan Kannan ◽  
Christian Doerig
Keyword(s):  
Protein Phosphorylation ◽  
Protein Kinases ◽  
Evolutionary Perspective ◽  
Malaria Parasites ◽  
Eukaryotic Protein ◽  
Independent Evolution ◽  
Ancient Lineage ◽  
Parasitic Lifestyle ◽  
Eukaryotic Protein Kinases

Malaria parasites belong to an ancient lineage that diverged very early from the main branch of eukaryotes. The approximately 90-member plasmodial kinome includes a majority of eukaryotic protein kinases that clearly cluster within the AGC, CMGC, TKL, CaMK and CK1 groups found in yeast, plants and mammals, testifying to the ancient ancestry of these families. However, several hundred millions years of independent evolution, and the specific pressures brought about by first a photosynthetic and then a parasitic lifestyle, led to the emergence of unique features in the plasmodial kinome. These include taxon-restricted kinase families, and unique peculiarities of individual enzymes even when they have homologues in other eukaryotes. Here, we merge essential aspects of all three malaria-related communications that were presented at the Evolution of Protein Phosphorylation meeting, and propose an integrated discussion of the specific features of the parasite's kinome and phosphoproteome.

The Structural Basis for Control of Eukaryotic Protein Kinases

2012 ◽  
Vol 81 (1) ◽  
pp. 587-613 ◽  
Author(s):  
Jane A. Endicott ◽  
Martin E.M. Noble ◽  
Louise N. Johnson
Keyword(s):  
Protein Kinases ◽  
Structural Basis ◽  
Eukaryotic Protein ◽  
Eukaryotic Protein Kinases

scholarly journals Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases

PLoS Biology ◽  
2016 ◽  
Vol 14 (11) ◽  
pp. e2000127 ◽  
Author(s):  
Hiruy S. Meharena ◽  
Xiaorui Fan ◽  
Lalima G. Ahuja ◽  
Malik M. Keshwani ◽  
Christopher L. McClendon ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Active State ◽  
Eukaryotic Protein ◽  
Eukaryotic Protein Kinases

scholarly journals EKPD: a hierarchical database of eukaryotic protein kinases and protein phosphatases

2013 ◽  
Vol 42 (D1) ◽  
pp. D496-D502 ◽  
Author(s):  
Yongbo Wang ◽  
Zexian Liu ◽  
Han Cheng ◽  
Tianshun Gao ◽  
Zhicheng Pan ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Protein Phosphatases ◽  
Eukaryotic Protein ◽  
Eukaryotic Protein Kinases
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