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calmodulin/oryza sativa

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C-terminal extension of calmodulin-like 3 protein from Oryza sativa L.: interaction with a high mobility group target protein.

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A large number of calmodulin-like (CML) proteins are present in plants, but there is little detailed information on the functions of these proteins in rice (Oryza sativa L.). Here, the CML3 protein from rice (OsCML3) and its truncated form lacking the C-terminal extension (OsCML3m) were found to

Expression analysis of calmodulin and calmodulin-like genes from rice, Oryza sativa L.

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BACKGROUND In plants, a large family of calmodulin (CaM) and CaM-like (CML) proteins transduce the increase in cytosolic Ca2+ concentrations by binding to and altering the activities of target proteins, and thereby affecting the physiological responses to a vast array of stimuli. Here, transcript

Calcium signaling-mediated and differential induction of calmodulin gene expression by stress in Oryza sativa L.

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Ca(2+)/calmodulin transduction pathways have been implicated in mediating stress response and tolerance in plants. Here, three genes encoding calmodulin (Cam) members of the EF-hand family of Ca(2+)-binding proteins were identified from Oryza sativa L. databases. Complementary DNA for each of the

Isolation of a calmodulin-binding transcription factor from rice (Oryza sativa L.).

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Calmodulin (CaM) regulates diverse cellular functions by modulating the activities of a variety of enzymes and proteins. However, direct modulation of transcription factors by CaM has been poorly understood. In this study, we isolated a putative transcription factor by screening a rice cDNA

Oscillation regulation of Ca2+ /calmodulin and heat-stress related genes in response to heat stress in rice (Oryza sativa L.).

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The Ca ( 2+) /calmodulin (CaM) signaling pathway mediates the heat stress (HS) response and acquisition of thermotolerance in plants. We showed that the rice CaM1-1 isoform can interpret a Ca ( 2+) signature difference in amplitude, frequency, and temporal-spatial properties in regulating

Biophysical characterization of calmodulin and calmodulin-like proteins from rice, Oryza sativa L.

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Calmodulin (CaM) transduces the increase in cytosolic Ca(2+) concentrations by binding to and altering the activities of target proteins, thereby affecting the physiological responses to the vast array of stimuli. Here, we examined the purified recombinant proteins encoded by three Cam and eight

Structure and expression analysis of the OsCam1-1 calmodulin gene from Oryza sativa L.

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Calmodulin (CaM) proteins, members of the EF-hand family of Ca(2+)- binding proteins, represent important relays in plant calcium signals. Here, OsCam1-1 was isolated by PCR amplification from the rice genome. The gene contains an ORF of 450 base pairs with a single intron at the same position found

Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus.

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We have isolated full-length cDNAs for two distinct isoforms of glutamate decarboxylase (GAD), designated OsGAD1 and OsGAD2 from a rice shoot cDNA library. Open reading frames found in OsGAD1 and OsGAD2 cDNAs encode putative proteins of 501 (56.7 kDa) and 500 amino acids (55.6 kDa), respectively.

Genome-wide comparative analysis of the IQD gene families in Arabidopsis thaliana and Oryza sativa.

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BACKGROUND Calcium signaling plays a prominent role in plants for coordinating a wide range of developmental processes and responses to environmental cues. Stimulus-specific generation of intracellular calcium transients, decoding of calcium signatures, and transformation of the signal into cellular

A tobacco (Nicotiana tabaccum) calmodulin-binding protein kinase, NtCBK2, is regulated differentially by calmodulin isoforms.

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A calcium (Ca2+)/calmodulin (CaM)-binding protein kinase (CBK) from tobacco (Nicotiana tabaccum ), NtCBK2, has been characterized molecularly and biochemically. NtCBK2 has all 11 conserved subdomains of the kinase-catalytic domain and a CaM-binding site as shown by other kinases, including

Structural analysis of a calmodulin variant from rice: the C-terminal extension of OsCaM61 regulates its calcium binding and enzyme activation properties.

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OsCaM61 is one of five calmodulins known to be present in Oryza sativa that relays the increase of cytosolic [Ca(2+)] to downstream targets. OsCaM61 bears a unique C-terminal extension with a prenylation site. Using nuclear magnetic resonance (NMR) spectroscopy we studied the behavior of the

Molecular and biochemical characterization of a calcium/calmodulin-binding protein kinase from rice.

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A Ca2+/calmodulin (CaM)-binding protein kinase from rice ( Oryza sativa ), OsCBK, has been characterized that lacks Ca2+-binding EF hands and has Ca2+/CaM-independent autophosphorylation and substrate-phosphorylation activity. OsCBK has all 11 subdomains of a kinase catalytic domain and a putative

Genome-wide identification and analyses of the rice calmodulin and related potential calcium sensor proteins.

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BACKGROUND A wide range of stimuli evoke rapid and transient increases in [Ca2+]cyt in plant cells which are transmitted by protein sensors that contain EF-hand motifs. Here, a group of Oryza sativa L. genes encoding calmodulin (CaM) and CaM-like (CML) proteins that do not possess functional domains

Possible roles of calcium and calmodulin in the biosynthesis and secretion of alpha-amylase in rice seed scutellar epithelium.

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The scutellar epithelial cells of rice (Oryza sativa L. cv Kimmazé) seeds actively secrete alpha-amylase in an early stage of germination. Employing an in vivo system of freshly dissected scutellar tissues, effect of Ca(2+) on the biosynthesis and the secretion of alpha-amylase have been studied.

Involvement of calcium-dependent protein kinase in rice (Oryza sativa L.) lamina inclination caused by brassinolide.

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Promotive effect of brassinolide (BL) on green lamina inclination was concentration-dependent when excised rice (Oryza sativa L.) lamina was floated on BL solution under continuous light conditions. Protein kinase inhibitor staurosporine and Ca2+ channel blocker LaCl3 could completely, while Ca2+
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