CBSXs are sensor relay proteins sensing adenosine-containing ligands in Arabidopsis

Plant Signaling and Behavior

Volumn 7, Issue 6, 2012, Pages 664-667

  Ok, Sung Han ^a   Yoo, Kyoung Shin ^a   Shin, Jeong Sheop ^a  

^a Korea University   (South Korea)

Author keywords

Adenosine containing ligand; CBS domain; CBSX; Redox; Sensor relay; Thioredoxin

Indexed keywords

ADENOSINE; ARABIDOPSIS PROTEIN; LIGAND;

ARABIDOPSIS; ARTICLE; BIOLOGICAL MODEL; BIOLOGY; METABOLISM; SIGNAL TRANSDUCTION;

ADENOSINE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; COMPUTATIONAL BIOLOGY; LIGANDS; MODELS, BIOLOGICAL; SIGNAL TRANSDUCTION;

ANIMALIA; ARABIDOPSIS; PROKARYOTA;

EID: 84863869111     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.19945     Document Type: Article

References (22)

1. Jonak C, Okrész L, Bögre L, Hirt H. Complexity, cross talk and integration of plant MAP kinase signalling. Curr Opin Plant Biol 2002; 5:415-24; PMID:12183180; http://dx.doi.org/10.1016/S1369-5266(02)00285-6.
2. Harper JF, Breton G, Harmon AC. Decoding Ca(2+) signals through plant protein kinases. Annu Rev Plant Biol 2004; 55:263-88; PMID:15377221; http://dx.doi.org/10.1146/annurev.arplant.55.031903.141627.
3. Kim MC, Panstruga R, Elliott C, Müller J, Devoto A, Yoon HW, et al. Calmodulin interacts with MLO protein to regulate defence against mildew in barley. Nature 2002; 416:447-51; PMID:11919636; http://dx.doi.org/10.1038/416447a.
4. Park CY, Lee JH, Yoo JH, Moon BC, Choi MS, Kang YH, et al. WRKY group IId transcription factors interact with calmodulin. FEBS Lett 2005; 579:1545-50; PMID:15733871; http://dx.doi. org/10.1016/j.febslet.2005.01.057.
5. Anandalakshmi R, Marathe R, Ge X, Herr JMJ Jr, Mau C, Mallory A, et al. A calmodulin-related protein that suppresses posttranscriptional gene silencing in plants. Science 2000; 290:142-4; PMID:11021800; http://dx.doi.org/10.1126/science.290.5489.142.
6. Oh SI, Park J, Yoon S, Kim Y, Park S, Ryu M, et al. The Arabidopsis calcium sensor calcineurin B-like 3 inhibits the 5'-methylthioadenosine nucleosidase in a calcium-dependent manner. Plant Physiol 2008; 148:1883-96; PMID:18945934; http://dx.doi. org/10.1104/pp.108.130419.
7. Kushwaha HR, Singh AK, Sopory SK, Singla-Pareek SL, Pareek A. Genome wide expression analysis of CBS domain containing proteins in Arabidopsis thaliana (L.) Heynh and Oryza sativa L. reveals their developmental and stress regulation. BMC Genomics 2009; 10:200-21; PMID:19400948; http://dx.doi. org/10.1186/1471-2164-10-200.
8. Yoo KS, Ok SH, Jeong BC, Jung KW, Cui MH, Hyoung S, et al. Single cystathionine β-synthase domain-containing proteins modulate development by regulating the thioredoxin system in Arabidopsis. Plant Cell 2011; 23:3577-94; PMID:22021414; http://dx.doi.org/10.1105/tpc.111.089847.
9. Johnson TC, Cao RQ, Kung JE, Buchanan BB. Thioredoxin and NADP-thioredoxin reductase from cultured carrot cells. Planta 1987; 171:321-31; PMID:11539727; http://dx.doi.org/10.1007/BF00398677.
10. Marcus F, Chamberlain SH, Chu C, Masiarz FR, Shin S, Yee BC, et al. Plant thioredoxin h: an animallike thioredoxin occurring in multiple cell compartments. Arch Biochem Biophys 1991; 287:195-8; PMID:1897989; http://dx.doi.org/10.1016/0003-9861(91)90406-9.
11. Rivera-Madrid R, Mestres D, Marinho P, Jacquot JP, Decottignies P, Miginiac-Maslow M, et al. Evidence for five divergent thioredoxin h sequences in Arabidopsis thaliana. Proc Natl Acad Sci USA 1995; 92:5620-4; PMID:7777559; http://dx.doi. org/10.1073/pnas.92.12.5620.
12. Gelhaye E, Rouhier N, Gérard J, Jolivet Y, Gualberto J, Navrot N, et al. A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase. Proc Natl Acad Sci USA 2004; 101:14545-50; PMID:15385674; http://dx.doi. org/10.1073/pnas.0405282101.
13. Juárez-Díaz JA, McClure B, Vázquez-Santana S, Guevara-García A, León-Mejía P, Márquez-Guzmán J, et al. A novel thioredoxin h is secreted in Nicotiana alata and reduces S-RNase in vitro. J Biol Chem 2006; 281:3418-24; PMID:16354655; http://dx.doi. org/10.1074/jbc.M511687200.
14. Montrichard F, Alkhalfioui F, Yano H, Vensel WH, Hurkman WJ, Buchanan BB. Thioredoxin targets in plants: the first 30 years. J Proteomics 2009; 72:452-74; PMID:19135183; http://dx.doi.org/10.1016/j. jprot.2008.12.002.
15. Tuominen H, Salminen A, Oksanen E, Jämsen J, Heikkilä O, Lehtiö L, et al. Crystal structures of the CBS and DRTGG domains of the regulatory region of Clostridium perfringens pyrophosphatase complexed with the inhibitor, AMP and activator, diadenosine tetraphosphate. J Mol Biol 2010; 398:410-3; http://dx.doi.org/10.1016/j.jmb.2010.03.019.
16. Jin X, Townley R, Shapiro L. Structural insight into AMPK regulation: ADP comes into play. Structure 2007; 15:1285-95; PMID:17937917; http://dx.doi. org/10.1016/j.str.2007.07.017.
17. Meyer S, Savaresi S, Forster IC, Dutzler R. Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5. Nat Struct Mol Biol 2007; 14:60-7; PMID:17195847; http://dx.doi.org/10.1038/nsmb1188.
18. Dong A, Xu X, Edwards AM, Chang C, Chruszcz M, Cuff M, et al.; Midwest Center for Structural Genomics; Structural Genomics Consortium. In situ proteolysis for protein crystallization and structure determination. Nat Methods 2007; 4:1019-21; PMID:17982461; http://dx.doi.org/10.1038/nmeth1118.
19. Lucas M, Encinar JA, Arribas EA, Oyenarte I, García IG, Kortazar D, et al. Binding of S-methyl-5'-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair. J Mol Biol 2010; 396:800-20; PMID:20026078; http://dx.doi. org/10.1016/j.jmb.2009.12.012.
20. Aguado-Llera D, Oyenarte I, Martínez-Cruz LA, Neira JL. The CBS domain protein MJ0729 of M. jannaschii binds DNA. FEBS Lett 2010; 584:4485-9; PMID:20934423; http://dx.doi.org/10.1016/j.febslet. 2010.10.006.
21. Ignoul S, Eggermont J. CBS domains: structure, function and pathology in human proteins. Am J Physiol Cell Physiol 2005; 289:1369-78; PMID:16275737; http://dx.doi.org/10.1152/ajpcell.00282.2005.
22. Baykov AA, Tuominen HK, Lahti R. The CBS domain: a protein module with an emerging prominent role in regulation. ACS Chem Biol 2011; 6:1156-63; PMID:21958115; http://dx.doi.org/10.1021/cb200231c.