scholarly journals Characterization of a Tomato Protein Kinase Gene Induced by Infection by Potato spindle tuber viroid

2000 ◽  
Vol 13 (9) ◽  
pp. 903-910 ◽  
Author(s):  
Rosemarie W. Hammond ◽  
Yan Zhao
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Catalytic Domain ◽  
Potato Spindle Tuber Viroid ◽  
Circular Rna ◽  
Sequence Motifs ◽  
Kinase Gene ◽  
Viroid Infection ◽  
Protein Kinase Gene

Viroids—covalently closed, circular RNA molecules in the size range of 250 to 450 nucleotides—are the smallest known infectious agents and cause a number of diseases of crop plants. Viroids do not encode proteins and replicate within the nucleus without a helper virus. In many cases, viroid infection results in symptoms of stunting, epinasty, and vein clearing. In our study of the molecular basis of the response of tomato cv. Rutgers to infection by Potato spindle tuber viroid (PSTVd), we have identified a specific protein kinase gene, pkv, that is transcriptionally activated in plants infected with either the intermediate or severe strain of PSTVd, at a lower level in plants inoculated with a mild strain, and not detectable in mock-inoculated plants. A full-length copy of the gene encoding the 55-kDa PKV (protein kinase viroid)-induced protein has been isolated and sequence analysis revealed significant homologies to cyclic nucleotide-dependent protein kinases. Although the sequence motifs in the catalytic domain suggest that it is a serine/threonine protein kinase, the recombinant PKV protein autophosphorylates in vitro on serine and tyrosine residues, suggesting that it is a putative member of the class of dual-specificity protein kinases.

Characterization of a dual plant protein kinase (FsPK1) up-regulated by abscisic acid and calcium and specifically expressed in dormant seeds ofFagus sylvaticaL.

2003 ◽  
Vol 13 (4) ◽  
pp. 261-271 ◽  
Author(s):  
O. Lorenzo ◽  
C. Nicolás ◽  
G. Nicolás ◽  
D. Rodríguez
Keyword(s):  
Abscisic Acid ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Catalytic Domain ◽  
Consensus Sequence ◽  
Calcium Dependent ◽  
Localization Signal ◽  
Rapid Amplification

An abscisic acid (ABA)-induced cDNA fragment encoding a putative protein kinase (PK) was obtained by differential screening of a cDNA library fromFagus sylvaticaseeds. The full-length clone, named FsPK1, was produced by 5′ rapid amplification of cDNA ends (RACE) extension. This clone contained the 11 catalytic domains present in all protein kinases, but displayed unusual characteristics found only in a few plant PKs. FsPK1 exhibits features of both serine/threonine and tyrosine protein kinases within the catalytic domain, a putative nuclear localization signal within the regulatory domain and the consensus sequence involved in binding of 14-3-3 proteins. The catalytic domain, expressed inEscherichia colias a fusion protein, showed Ca2+-dependentin vitrokinase activity and dual serine/threonine and tyrosine specificity. Transcription of theFsPK1gene was reduced by seed stratification at 4°C, and clearly increased when seeds were treated with 0.1 mM ABA, correlating with the inhibition of germination. Interestingly,FsPK1transcripts were enhanced when ABA (0.1 mM) and calcium (1 mM) were added together, while the addition of EGTA (calcium chelator) and 3,4,5,-trimethoxibenzoic acid 8-(diethylamino) octyl ester (TMB-8, a calcium antagonist) decreased its expression. Furthermore,FsPK1transcript expression was tissue specific and accumulated only in ABA-treated seeds, but not in any ABA-treated vegetative tissues examined. These results suggest that the expression of the corresponding protein could be related to the inhibition of germination mediated by ABA in a calcium-dependent pathway.

scholarly journals Molecular cloning of a second form of rac protein kinase.

1991 ◽  
Vol 2 (12) ◽  
pp. 1001-1009 ◽  
Author(s):  
P F Jones ◽  
T Jakubowicz ◽  
B A Hemmings
Keyword(s):  
Amino Acids ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Cell Lines ◽  
Catalytic Domain ◽  
Cell Types ◽  
In Vitro Translation ◽  
Cdna Libraries ◽  
Beta Form

A novel serine/threonine protein kinase (termed rac-PK) has recently been identified and cloned from cDNA libraries derived from the human cell lines MCF-7 and WI38. A second form of this protein kinase, termed rac protein kinase beta, has been identified from cDNAs derived from the same cell lines. These two closely related forms show 90% homology, although the beta form with a predicted Mr 60,200 has a carboxyl terminal extension of 40 amino acids in comparison to the alpha form. This extension has a high serine content with 11 serine residues in the last 30 amino acids. The beta form of the protein has been shown by both in vitro translation and bacterial expression to be approximately 5000 Da larger than the alpha form. rac protein kinase beta is encoded by a 3.4-kb transcript and the alpha form is encoded by a 3.2-kb mRNA. Using gene-specific probes both transcripts were detected in all cell types analyzed, although levels of expression were different for the two forms. The catalytic domain of rac protein kinase beta shows a high degree of homology to both the protein kinase C and cyclic AMP-dependent protein kinase families, and hence rac protein kinases appear to represent a new subfamily of the second messenger serine/threonine protein kinases.

Characterization of a protein kinase gene from two Chlorella viruses

1995 ◽  
Vol 35 (3) ◽  
pp. 291-305 ◽  
Author(s):  
Quideng Que ◽  
James L. Van Etten
Keyword(s):  
Protein Kinase ◽  
Kinase Gene ◽  
Protein Kinase Gene

scholarly journals Negative control of Candida albicans filamentation-associated gene expression by essential protein kinase gene KIN28

2017 ◽  
Vol 63 (6) ◽  
pp. 1073-1079 ◽  
Author(s):  
C. A. Woolford ◽  
K. Lagree ◽  
T. Aleynikov ◽  
A. P. Mitchell
Keyword(s):  
Gene Expression ◽  
Candida Albicans ◽  
Protein Kinase ◽  
Negative Control ◽  
Kinase Gene ◽  
Essential Protein ◽  
Protein Kinase Gene

scholarly journals The Evolutionary History and Diverse Physiological Roles of the Grapevine Calcium-Dependent Protein Kinase Gene Family

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e80818 ◽  
Author(s):  
Fei Chen ◽  
Marianna Fasoli ◽  
Giovanni Battista Tornielli ◽  
Silvia Dal Santo ◽  
Mario Pezzotti ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Gene Family ◽  
Evolutionary History ◽  
Dependent Protein Kinase ◽  
Kinase Gene ◽  
Calcium Dependent ◽  
Dependent Protein ◽  
Protein Kinase Gene ◽  
Calcium Dependent Protein Kinase

Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK

2001 ◽  
Vol 355 (2) ◽  
pp. 297-305 ◽  
Author(s):  
Diana L. LEFEBVRE ◽  
Yahong BAI ◽  
Nazanin SHAHMOLKY ◽  
Monika SHARMA ◽  
Raymond POON ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cellular Response ◽  
Catalytic Domain ◽  
Metabolic Stress ◽  
Glucose Deprivation ◽  
Protein Band ◽  
Northern Blotting ◽  
Significant Similarity ◽  
Amp Activated Protein Kinase

Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.

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