Calcium-dependent protein kinase genes in corn roots

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

doi:10.1016/s0176-1617(96)80130-1

Cited by 12 publications

(4 citation statements)

References 33 publications

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“…The sorghum homolog with the closest sequence similarity to OsPSTOL1 was Sb07g002840, which is located on sorghum chromosome 7, and another five highly similar homologs are located on sorghum chromosome 3. Similar to OsPSTOL1, all six sorghum PSTOL1 proteins (SbPSTOL1) are predicted to have a Ser/Thr kinase domain (Pfam identifier PF00069.18) and are members of the Corn root protein kinase1 family (CRPK1) (Takezawa et al, 1996).…”

Section: Identification Of Pstol1 Homologs In Sorghum and Snp Discoverymentioning

confidence: 99%

Duplicate and Conquer: Multiple Homologs ofPHOSPHORUS-STARVATION TOLERANCE1Enhance Phosphorus Acquisition and Sorghum Performance on Low-Phosphorus Soils

et al. 2014

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Low soil phosphorus (P) availability is a major constraint for crop production in tropical regions. The rice (Oryza sativa) protein kinase, PHOSPHORUS-STARVATION TOLERANCE1 (OsPSTOL1), was previously shown to enhance P acquisition and grain yield in rice under P deficiency. We investigated the role of homologs of OsPSTOL1 in sorghum (Sorghum bicolor) performance under low P. Association mapping was undertaken in two sorghum association panels phenotyped for P uptake, root system morphology and architecture in hydroponics and grain yield and biomass accumulation under low-P conditions, in Brazil and/or in Mali. Root length and root surface area were positively correlated with grain yield under low P in the soil, emphasizing the importance of P acquisition efficiency in sorghum adaptation to low-P availability. SbPSTOL1 alleles reducing root diameter were associated with enhanced P uptake under low P in hydroponics, whereas Sb03g006765 and Sb03g0031680 alleles increasing root surface area also increased grain yield in a low-P soil. SbPSTOL1 genes colocalized with quantitative trait loci for traits underlying root morphology and dry weight accumulation under low P via linkage mapping. Consistent allelic effects for enhanced sorghum performance under low P between association panels, including enhanced grain yield under low P in the soil in Brazil, point toward a relatively stable role for Sb03g006765 across genetic backgrounds and environmental conditions. This study indicates that multiple SbPSTOL1 genes have a more general role in the root system, not only enhancing root morphology traits but also changing root system architecture, which leads to grain yield gain under low-P availability in the soil.

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Section: Identification Of Pstol1 Homologs In Sorghum and Snp Discoverymentioning

confidence: 99%

Duplicate and Conquer: Multiple Homologs ofPHOSPHORUS-STARVATION TOLERANCE1Enhance Phosphorus Acquisition and Sorghum Performance on Low-Phosphorus Soils

et al. 2014

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“…The peculiarity arises from the fact that the activation of CDPK is independent of CaM or phospholipids, and as such, these proteins, first isolated from suspension‐cultured soybean cells, represent a new class of protein kinases 4. An incomplete list includes CDPKs identified in the higher plants Arabidopsis, 5, 6 carrot,7 rice,8 groundnut seeds,9 corn,10 wheat,11 mungbean,12 the protozoan Plasmodium falciparum, 13, 14 and the green algae Chara 15 and Gerloff 16…”

Section: Introductionmentioning

confidence: 99%

Comparative modeling studies of the calmodulin-like domain of calcium-dependent protein kinase from soybean

et al. 2000

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Calmodulin-like domain protein kinases (CDPKs) represent a new class of calcium-dependent protein-phosphorylating enzymes that are not activated by calmodulin or phospholipid compounds. They have been found exclusively in plant and protozoal tissues. CDPKs are typified by four distinct domains: an N-terminal leader sequence, a protein kinase (PK) domain, a calmodulin-like domain (CLD), and a junction domain (JD) between the PK domain and CLD. Structural characterization of the CLD of CDPKalpha from soybean was undertaken based on the amino acid sequence homology of CLD to the structurally well-characterized calmodulin (CaM) family of structures. Tertiary models of apo-CLD, Ca(2+)-CLD complex, and intermolecularly bound Ca(2+)-CLD-JD complexes were obtained via automated and non-automated homology building methods. The resulting structures were compared and validated based on energy differences, phi-psi angle distribution, solvent accessibility, and hydrophobic potential. Circular dichroism, one-dimensional, and two-dimensional nuclear magnetic resonance spectroscopy studies of the CLD and peptides encompassing the JD provide experimental support to the models. The results suggest that there is a possible interaction between the CLD and JD domain similar to that of the CaM/calmodulin-dependent protein kinase II system. At low Ca(2+) levels, the JD may act as an autoinhibitory domain for kinase activity, and during calcium activation an intramolecular CLD-JD complex may form, relieving inhibition of the PK domain. Interactions between the JD and the C terminus of the CLD appear to be particularly important. The outcome of this study supports an intramolecular binding model for calcium activation of CDPK, although not exclusively.

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“…7A), there is no significant sequence similarity outside of their kinase domains. CRPK2 is a typical form of CDPK and has extensive and significant homology to other CDPKs (16). The amino acid sequence of CRPK2 shares 75% similarity and 65% identity with the prototype of CDPK, soybean CDPK␣, along their three functional domains (kinase domain, junction domain, and CaM-like domain) (11).…”

Section: Resultsmentioning

confidence: 99%

Interaction of Plant Chimeric Calcium/Calmodulin-dependent Protein Kinase with a Homolog of Eukaryotic Elongation Factor-1α

Wang

Poovaiah

1999

Journal of Biological Chemistry

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A chimeric Ca2؉ /calmodulin-dependent protein kinase (CCaMK) was previously cloned and characterized in this laboratory. To investigate the biological functions of CCaMK, the yeast two-hybrid system was used to isolate genes encoding proteins that interact with CCaMK. One of the cDNA clones obtained from the screening (LlEF-1␣1) has high similarity with the eukaryotic elongation factor-1␣ (EF-1␣

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Calcium-dependent protein kinase genes in corn roots

Cited by 12 publications

References 33 publications

Duplicate and Conquer: Multiple Homologs ofPHOSPHORUS-STARVATION TOLERANCE1Enhance Phosphorus Acquisition and Sorghum Performance on Low-Phosphorus Soils

Duplicate and Conquer: Multiple Homologs ofPHOSPHORUS-STARVATION TOLERANCE1Enhance Phosphorus Acquisition and Sorghum Performance on Low-Phosphorus Soils

Comparative modeling studies of the calmodulin-like domain of calcium-dependent protein kinase from soybean

Interaction of Plant Chimeric Calcium/Calmodulin-dependent Protein Kinase with a Homolog of Eukaryotic Elongation Factor-1α

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