DOI QR코드

DOI QR Code

Identification of another calmodulin-binding domain at the C-terminal region of AtCBP63

  • Kim, Sun-Ho (Environmental Biotechnology National Core Research Center, Gyeongsang National University) ;
  • Kang, Yun-Hwan (Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University) ;
  • Han, Hay-Ju (Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University) ;
  • Bae, Dong-Won (Central Instrument Facility, Gyeongsang National University) ;
  • Kim, Min-Chul (Environmental Biotechnology National Core Research Center, Gyeongsang National University) ;
  • Lim, Chae-Oh (Environmental Biotechnology National Core Research Center, Gyeongsang National University) ;
  • Chung, Woo-Sik (Environmental Biotechnology National Core Research Center and Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University)
  • Published : 2009.03.31

Abstract

Calcium signals can be transduced by binding calmodulin (CaM), a $Ca^{2+}$ sensor in eukaryotes, is known to be involved in the regulation of diverse cellular functions. We isolated a CaM-binding protein 63 kD (AtCBP63) from the pathogen-treated Arabidopsis cDNA expression library. Recently, AtCBP63 was identified as a CaM bining protein. The CaM binding domain of AtCBP63 was reported to be located in its N-terminal region, In this study, however, we showed that ACaM2 could specifically bind to second CaM-binding domain (CaMBD) of AtCBP63 at the C-terminal region. The specific binding of CaM to CaM binding domain was confirmed by a gel mobility shift assay, a split ubiquitin assay, site-directed mutagenesis, and a competition assay using a $Ca^{2+}$/CaM-dependent enzyme. The gene expression of AtCBP63 was induced by pathogens and pathogens related second messengers. This result suggests that a CaM binding protein, AtCBP63, may play role in pathogen defense signaling pathway.

Keywords

References

  1. Bush DS (1995) Calcium Regulation in Plant Cells and its Role in Signaling. Annu Rev Plant Mol Biol 46:95-122 https://doi.org/10.1146/annurev.pp.46.060195.000523
  2. Dolmetsch RE, Lewis RS, Goodnow CC, Healy JI (1997) Differential activation of transcription factors induced by $Ca^{2+}$ response amplitude and duration. Nature 24:855-858 https://doi.org/10.1038/386855a0
  3. Du L, Poovaiah BW (2004) A novel family of $Ca^{2-}$/calmodulinbinding proteins involved in transcriptional regulation: interaction with fsh/Ring3 class transcription activators. Plant Mol Biol 54:639-569 https://doi.org/10.1023/B:PLAN.0000038269.98972.bb
  4. Erickson-Vitanen S, DeGrado WF (1987) Recognition and characterization of calmodulin-binding sequences in peptide and proteins. Methods Enzymol 139:455-478 https://doi.org/10.1016/0076-6879(87)39106-2
  5. Hoeflich KP, Ikura M (2002) Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108:739-742 https://doi.org/10.1016/S0092-8674(02)00682-7
  6. James P, Vorherr T, Carafoli E (1995) Calmodulin-binding domains: just two faced or multi-faceted? Trends Biochem Sci 20:38-42 https://doi.org/10.1016/S0968-0004(00)88949-5
  7. Kim HS, Park BO, Yoo JH, Jung MS, Lee SM, Han HJ, Kim KE, Kim SH, Lim CO, Yun DJ, Lee SY, Chung WS (2007) Identification of a calmodulin-binding NAC protein as a transcriptional repressor in Arabidopsis. J Biol Chem 282:36292-36302 https://doi.org/10.1074/jbc.M705217200
  8. Knight MR, Campbell AK, Smith SM, Trewavas AJ (1991) Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium. Nature 352:524-526 https://doi.org/10.1038/352524a0
  9. Laser H, Bongards C, Schuller J, Heck S, Johnsson N, Lehming H (2000) A new screen for protein interactions reveals that the Saccharomyces cerevisiae high mobility group proteins Nhp6A/B are involved in the regulation of the GAL1 promoter. Proc Natl Acad Sci USA 97:13732-13737 https://doi.org/10.1073/pnas.250400997
  10. Lee K, Song EH, Kim HS, Yoo JH, Han HJ, Jung MS, Lee SM, Kim KE, Kirn MC, Cho MJ, Chung WS (2008) Regulation of MAPK phosphatase 1 (AtMKPl) by calmodulin in Arabidopsis. J Biol Chem 283:23581-23588 https://doi.org/10.1074/jbc.M801549200
  11. Lee SH, Johnson JD, Walsh MP, Van Lierop JE, Sutherland C, Xu A, Snedden WA, Kosk-Kosicka D, Fromm H, Narayanan N, Cho, MJ (2000) Differential regulation of $Ca^{2+}$/calmodulin-dependent enzymes by plant calmodulin isoforms and free $Ca^{2+}$ concentration. Biochem J 1:299-306 https://doi.org/10.1042/0264-6021:3500299
  12. Lee SH, Kim MC, Heo WD, Kim JC, Chung WS, Park CY, Park HC, Cheong YH, Kim CY, Lee KJ, Bahk JD, Lee SY, Cho MJ (1999) Competitive binding of calmodulin isoforms to calmodulin-binding proteins: implication for the function of calmodulin isoforms in plants. Biochim Biophys Acta 1433:56-67 https://doi.org/10.1016/S0167-4838(99)00149-1
  13. Lee SM, Kim HS, Han HJ, Moon BC, Kim CY, Harper JF, Chung WS (2007) Identification of a calmodulin-regulated autoinhibited $Ca^{2+}$-ATPase (ACA11) that is localized to vacuole membranes in Arabidopsis. FEBS Lett 581:3943-3949 https://doi.org/10.1016/j.febslet.2007.07.023
  14. McAinsh MR, Hetherington AM (1998) Encoding specificity in $Ca^{2+}$ signalling systems. Trends Plant Sci 3:32-36 https://doi.org/10.1016/S1360-1385(97)01150-3
  15. McCormack E, Tsai YC, Braam J (2005) Handling calcium signaling: Arabidopsis CaMs and CMLs. Trends Plants Sci 10:383-389 https://doi.org/10.1016/j.tplants.2005.07.001
  16. Price AH, Taylor A, Ripley SJ, Griffiths A, Trewavas AJ, Knight MR (1994) Oxidative Signals in Tobacco Increase Cytosolic Calcium. Plant Cell 6:1301-1310 https://doi.org/10.1105/tpc.6.9.1301
  17. Reddy AS (2001) Calcium: silver bullet in signaling. Plant Sci 160:381-404 https://doi.org/10.1016/S0168-9452(00)00386-1
  18. Reddy VS, Reddy AS (2004) Proteomics of calcium-signaling components in plants. Phytochemistry 65:1745-1776 https://doi.org/10.1016/j.phytochem.2004.04.033
  19. Reddy VS, Safadi F, Zielinski RE, Reddy AS (1999) Interaction of a kinesin-like protein with calmodulin isoforms from Arabidopsis. J Biol Chem 274:31727-31733 https://doi.org/10.1074/jbc.274.44.31727
  20. Rhoads AR, Friedberg F (1997) Sequence motifs for calmodulin recognition. FASEB J 11:331-340 https://doi.org/10.1096/fasebj.11.5.9141499
  21. Sambrook J. Russell DW (2001) Molecular Cloning. A Laboratory Manual, Ed 3. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
  22. Snedden WA, Fromm H (2001) Calmodulin as a versatile calcium signal transducer in plants. New Phytol 151:35-66 https://doi.org/10.1046/j.1469-8137.2001.00154.x
  23. Stagljar I, Korostensky C, Johnsson N, Heesen S (1998) A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc Natl Acad Sci USA 95:5187-5192 https://doi.org/10.1073/pnas.95.9.5187
  24. Trewavas AJ, Malho R (1998) $Ca^{2+}$ signalling in plant cells: the big network! Curr. Opin. Plant Biol 1:428-433 https://doi.org/10.1016/S1369-5266(98)80268-9
  25. Wang L, Tsuda K, Sato M, Cohen JD, Katagiri F, Glazebrook J (2009) Arabidopsis CaM binding protein CBP60g contributes to MAMP-induced SA accumulation and is involved in disease resistance against Pseudomonas syringae. Plospathogen 5:1-14
  26. Yoo JH, Park CY, Kim JC, Heo WD, Cheong MS, Park HC, Kim MC, Moon BC, Choi MS, Kang YH, Lee JH, Kim HS, Lee SM, Yoon HW, Lim CO, Yun DJ, Lee SY, Chung WS, Cho MJ (2005) Dir+ect interaction of a divergent CaM isoform and the transcription factor, MYB2, enhances salt tolerance in Arabidopsis. J Biol Chem 280:3697-3706 https://doi.org/10.1074/jbc.M408237200

Cited by

  1. AtCBP63, a Arabidopsis Calmodulin-binding Protein 63, Enhances Disease Resistance Against Soft Rot Disease in Potato vol.38, pp.1, 2011, https://doi.org/10.5010/JPB.2011.38.1.062
  2. Agronomic characteristics and field resistance to bacterial soft rot of transgenic potato overexpressing the soybean calmodulin 4 gene (SCaM4) vol.39, pp.4, 2012, https://doi.org/10.5010/JPB.2012.39.4.295