Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain.

Patil, Shameekumar; Takezawa, Daisuke; Poovaiah, B. W.

doi:10.1073/pnas.92.11.4897

Cited by 158 publications

(138 citation statements)

References 36 publications

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“…The C-terminal domain of CDPKs and CCaMKs contains calcium-binding EF-hands resembling those found in either calmodulin (CDPKs;Harper et al, 1991) or visinin (CCaMKs; Patil et al, 1995). Calcium binding to the EF hands increases kinase activity.…”

Section: Resultsmentioning

confidence: 99%

“…CCaMKs have been cloned from tobacco and lily (Patil et al, 1995;, but they are apparently absent from Arabidopsis. The arrangement of functional domains in these enzymes is similar to that of the CDPKs, but the structure of their calciumbinding regulatory domain is more similar to visinin than to calmodulin and contains only three EF hands (Harmon et al, 1987;Patil et al, 1995;Yuasa et al, 1995;Pandey and Sopory, 1998).…”

Section: Camk and Ccamkmentioning

confidence: 99%

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The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases

Hrabak

Chan²,

Gribskov³

et al. 2003

Plant Physiology

909

823

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The CDPK-SnRK superfamily consists of seven types of serine-threonine protein kinases: calcium-dependent protein kinase (CDPKs), CDPK-related kinases (CRKs), phosphoenolpyruvate carboxylase kinases (PPCKs), PEP carboxylase kinase-related kinases (PEPRKs), calmodulin-dependent protein kinases (CaMKs), calcium and calmodulin-dependent protein kinases (CCaMKs), and SnRKs. Within this superfamily, individual isoforms and subfamilies contain distinct regulatory domains, subcellular targeting information, and substrate specificities. Our analysis of the Arabidopsis genome identified 34 CDPKs, eight CRKs, two PPCKs, two PEPRKs, and 38 SnRKs. No definitive examples were found for a CCaMK similar to those previously identified in lily (Lilium longiflorum) and tobacco (Nicotiana tabacum) or for a CaMK similar to those in animals or yeast. CDPKs are present in plants and a specific subgroup of protists, but CRKs, PPCKs, PEPRKs, and two of the SnRK subgroups have been found only in plants. CDPKs and at least one SnRK have been implicated in decoding calcium signals in Arabidopsis. Analysis of intron placements supports the hypothesis that CDPKs, CRKs, PPCKs and PEPRKs have a common evolutionary origin; however there are no conserved intron positions between these kinases and the SnRK subgroup. CDPKs and SnRKs are found on all five Arabidopsis chromosomes. The presence of closely related kinases in regions of the genome known to have arisen by genome duplication indicates that these kinases probably arose by divergence from common ancestors. The PlantsP database provides a resource of continuously updated information on protein kinases from Arabidopsis and other plants.In eukaryotes, protein kinases are involved in regulating key aspects of cellular function, including cell division, metabolism, and responses to external signals. The completed sequence of the Arabidopsis genome provides the first opportunity to identify all of the protein kinases present in a model plant. The Arabidopsis genome encodes 1,085 typical protein kinases (M. Gribskov, unpublished data), which is about 4% of the predicted 25,500 genes (Arabidopsis Article, publication date, and citation information can be found at www.plantphysiol.org/cgi

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Section: Resultsmentioning

confidence: 99%

Section: Camk and Ccamkmentioning

confidence: 99%

The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases

Hrabak

Chan²,

Gribskov³

et al. 2003

Plant Physiology

909

823

View full text Add to dashboard Cite

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“…To understand calmodulin-regulated processes, various strategies have been used to isolate, identify, and characterize the proteins that interact with calmodulin. These studies have resulted in identification of a few calmodulin-modulated proteins such as NAD kinase, calcium ATPase, nuclear nucleoside triphosphatase, a vacuolar ion channel, glutamate decarboxylase, elongation factor-1␣, and protein kinases in plants (1,(21)(22)(23)(24)(25)(26). Complementary DNAs that encode calmodulin-binding proteins of unknown function have also been isolated from maize and tobacco (27,28).…”

mentioning

confidence: 99%

A Novel Plant Calmodulin-binding Protein with a Kinesin Heavy Chain Motor Domain

Reddy

Safadi

Narasimhulu

et al. 1996

Journal of Biological Chemistry

169

155

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Calmodulin, a ubiquitous calcium-binding protein, regulates many diverse cellular functions by modulating the activity of the proteins that interact with it. Here, we report isolation of a cDNA encoding a novel kinesin-like calmodulin-binding protein (KCBP) from Arabidopsis using biotinylated calmodulin as a probe. Calcium-dependent binding of the cDNA-encoded protein to calmodulin is confirmed by 35

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“…The CCaMK gene from lily anthers is a chimeric gene in which a neural-visinin-like Ca 2ϩ -binding domain is fused with a CaM-binding domain. The Nterminal region of the encoded protein contains all eleven conserved subdomains characteristic of serine/threonine protein kinases, and the CaM-binding region has high similarity (79 %) to a subunit of mammalian CCaMK [38]. The cDNA clone from lily anthers has been over expressed in Escherichia coli, and its biochemical properties indicate it to be a CCaMK regulated by Ca 2ϩ and Ca 2ϩ /CaM [39].…”

mentioning

confidence: 99%

“…apple [35Ϫ37], lily [38,39], and maize [40]. All these homologues show considerable similarity with their animal counterparts at cDNA level.…”

mentioning

confidence: 99%

Biochemical evidence for a calmodulin‐stimulated calcium‐dependent protein kinase in maize

Pandey

Sopory

1998

European Journal of Biochemistry

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We provide biochemical evidence for the presence of a Ca 2ϩ -dependent calmodulin (CaM)-stimulated protein kinase (CCaMK) from etiolated maize coleoptiles. The kinase, with a molecular mass of 72.3 kDa, was purified to homogeneity by means of ammonium sulphate precipitation, DEAE-Sephacel chromatography, CaM-Sepharose chromatography and gel purification. The purified kinase required 5 mM Mg 2ϩ for activity and had an optimum pH of 7.5. The kinase is a Ca 2ϩ -binding protein, as was evident by 45 Ca 2ϩ -binding and Ca 2ϩ mobility-gel-shift assays. 1 µM Ca 2ϩ stimulated the kinase activity about 12-fold and was further stimulated by the addition of exogenous CaM (Ϸ100 nM). Addition of Ca 2ϩ and CaM antagonists decreased the kinase activity. Under in vitro assay conditions the kinase phosphorylated preferentially syntide-2, histone IIIS and casein. Syntide-2 and histone IIIS were phosphorylated at serine residues, showing that the kinase belongs to the serine/threonine family of protein kinases. Autophosphorylation of CCaMK occurred on threonine residue(s) and was Ca 2ϩ dependent. Addition of exogenous CaM had no effect on autophosphorylation. The properties of the maize kinase suggests that it is a CCaMK that shows dual stimulation with Ca 2ϩ and CaM for substrate phosphorylation and only Ca 2ϩ requirement for autophosphorylation. Antibodies raised against the kinase cross-reacted with maize total proteins to give a single band of 72 kDa and precipitated substrate (syntide-2 and histone IIIS)-phosphorylation and autophosphorylation activities in a specific manner. Localisation studies with antibodies showed that the kinase is ubiquitous.Keywords : calmodulin; Ca 2ϩ /calmodulin-dependent kinase ; Zea mays; protein kinase. Ca 2ϩ are one of the most common second messengers, and couple a large number of diverse stimuli to their characteristic responses in a very specific and precise manner in plant and animal systems [1Ϫ3]. In animal systems, the role of Ca 2ϩ as a second messenger has been very well established. Changes in intracellular Ca 2ϩ levels are perceived by various Ca 2ϩ -binding proteins, e.g. calmodulin (CaM) and CaM-like proteins, which either by themselves or by modifying other proteins and/or factors transduce the signal downstream to elicit the final response. Protein kinases are one of the main targets of these proteins, which by their reversible phosphorylation/dephosphorylation activate other constituents of signal-transduction pathways [1, 4Ϫ5].Ca 2ϩ is known to regulate two families of protein kinases, i.e. Ca 2ϩ /phospholipid-dependent protein kinases [6] and Ca 2ϩ / CaM-dependent protein kinases (CCaMK) [7Ϫ9]. In animal systems, various members of these families have been purified, and characterised, and their regulation has been understood [10]. In plants a third, biochemically distinct family of protein kinases, Ca 2ϩ -dependent protein kinases, is more common [11]. These kinases do not require lipid or CaM for their activation. These kinases are single polypeptides, containing conserved cata...

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Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain.

Abstract: Calcium, a universal second messenger, regulates diverse cellular processes in eukaryotes.

Cited by 158 publications

References 36 publications

The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases

The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases

A Novel Plant Calmodulin-binding Protein with a Kinesin Heavy Chain Motor Domain

Biochemical evidence for a calmodulin‐stimulated calcium‐dependent protein kinase in maize

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