The non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase

Journal of Biological Chemistry

Volumn 290, Issue 28, 2015, Pages 17559-17565

  Zhang, Min ^a   Zhang, Feilong ^a   Fang, Ying ^b,c   Chen, Xuemin ^b,c   Chen, Yuhong ^b   Zhang, Wenxia ^b   Dai, Huai En ^b   Lin, Rongcheng ^b   Liu, Lin ^b  

^a ANHUI UNIVERSITY   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; ENZYMES; PROTEINS;

AMINOLEVULINIC ACID; CHLOROPHYLL BIOSYNTHESIS; COMPLEX FORMATIONS; FUNCTIONAL UNITS; NEGATIVE REGULATORS; RATE-LIMITING ENZYMES; TETRATRICOPEPTIDE REPEAT DOMAINS; TETRATRICOPEPTIDE REPEATS;

BIOSYNTHESIS;

AMINOLEVULINIC ACID; FLUORESCENT PROTEIN; GLUTAMYL TRANSFER RNA REDUCTASE; MEMBRANE PROTEIN; OXIDOREDUCTASE; TETRATRICOPEPTIDE REPEAT PROTEIN; UNCLASSIFIED DRUG; ALDEHYDE DEHYDROGENASE; ARABIDOPSIS PROTEIN; FLU PROTEIN, ARABIDOPSIS; GLUTAMYL TRNA REDUCTASE; MULTIPROTEIN COMPLEX; TETRAPYRROLE DERIVATIVE;

AMINO ACID SYNTHESIS; ARABIDOPSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME REGULATION; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN QUATERNARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ALDEHYDE OXIDOREDUCTASES; AMINO ACID SEQUENCE; AMINOLEVULINIC ACID; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; REPETITIVE SEQUENCES, AMINO ACID; SEQUENCE HOMOLOGY, AMINO ACID; TETRAPYRROLES;

EID: 84940063497     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.662981     Document Type: Article

References (31)

1. Meskauskiene, R., Nater, M., Goslings, D., Kessler, F., op den Camp, R., and Apel, K. (2001) FLU: a negative regulator of chlorophyll biosynthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U.S.A. 98, 12826-12831
2. Meskauskiene, R., and Apel, K. (2002) Interaction of FLU, a negative regulator of tetrapyrrole biosynthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU. FEBS Lett. 532, 27-30
3. Falciatore, A., Merendino, L., Barneche, F., Ceol, M., Meskauskiene, R., Apel, K., and Rochaix, J. D. (2005) The FLP proteins act as regulators of chlorophyll synthesis in response to light and plastid signals in Chlamydomonas. Genes Dev. 19, 176-187
4. Lee, K. P., Kim, C., Lee, D. W., and Apel, K. (2003) TIGRINA d, required for regulating the biosynthesis of tetrapyrroles in barley, is an ortholog of the FLU gene of Arabidopsis thaliana. FEBS Lett. 553, 119-124
5. von Wettstein, D. V., Kahn, A., Nielsen, O. F., and Gough, S. (1974) Genetic regulation of chlorophyll synthesis analyzed with mutants in barley. Science 184, 800-802
6. Kumar, A. M., and Söll, D. (2000) Antisense HEMA1 RNA expression inhibits heme and chlorophyll biosynthesis in Arabidopsis. Plant Physiol. 122, 49-56
7. Goslings, D., Meskauskiene, R., Kim, C., Lee, K. P., Nater, M., and Apel, K. (2004) Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1), the target of metabolic feedback inhibition of tetrapyrrole biosynthesis, in dark- and light-grown Arabidopsis plants. Plant J. 40, 957-967
8. Moser, J., Schubert, W. D., Beier, V., Bringemeier, I., Jahn, D., and Heinz, D. W. (2001) V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis. EMBO J. 20, 6583-6590
9. Zhao, A., Fang, Y., Chen, X., Zhao, S., Dong, W., Lin, Y., Gong, W., and Liu, L. (2014) Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein. Proc. Natl. Acad. Sci. U.S.A. 111, 6630-6635
10. Tanaka, R., and Tanaka, A. (2007) Tetrapyrrole biosynthesis in higher plants. Annu. Rev. Plant Biol. 58, 321-346
11. Mochizuki, N., Tanaka, R., Grimm, B., Masuda, T., Moulin, M., Smith, A. G., Tanaka, A., and Terry, M. J. (2010) The cell biology of tetrapyrroles: a life and death struggle. Trends Plant Sci. 15, 488-498
12. Vothknecht, U. C., Kannangara, C. G., and von Wettstein, D. (1998) Barley glutamyl tRNAGlu reductase: mutations affecting haem inhibition and enzyme activity. Phytochemistry 47, 513-519
13. Richter, A., Peter, E., Pörs, Y., Lorenzen, S., Grimm, B., and Czarnecki, O. (2010) Rapid dark repression of 5-aminolevulinic acid synthesis in green barley leaves. Plant Cell Physiol. 51, 670-681
14. Kauss, D., Bischof, S., Steiner, S., Apel, K., and Meskauskiene, R. (2012) FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is physically linked to the final steps of the Mg++-branch of this pathway. FEBS Lett. 586, 211-216
15. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., and Read, R. J. (2007) Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674
16. Zhu, J., Wen, W., Zheng, Z., Shang, Y., Wei, Z., Xiao, Z., Pan, Z., Du, Q., Wang, W., and Zhang, M. (2011) LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in asymmetric cell division for the Par3/mInsc/LGN and Gαi/LGN/NuMA pathways. Mol. Cell 43, 418-431
17. Perrakis, A., Harkiolaki, M., Wilson, K. S., and Lamzin, V. S. (2001) ARP/wARP and molecular replacement. Acta Crystallogr. D 57, 1445-1450
18. Emsley, P., Lohkamp, B., Scott, W. G., and Cowtan, K. (2010) Features and development of Coot. Acta Crystallogr. D 66, 486-501
19. Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., and Adams, P. D. (2012) Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D 68, 352-367
20. Chen, V. B., Arendall, W. B., 3rd, Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21
21. Das, A. K., Cohen, P. W., and Barford, D. (1998) The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17, 1192-1199
22. D'Andrea, L. D., and Regan, L. (2003) TPR proteins: the versatile helix. Trends Biochem. Sci. 28, 655-662
23. Grove, T. Z., Cortajarena, A. L., and Regan, L. (2008) Ligand binding by repeat proteins: natural and designed. Curr. Opin. Struct. Biol. 18, 507-515
24. Zeytuni, N., and Zarivach, R. (2012) Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module. Structure 20, 397-405
25. op den Camp, R. G., Przybyla, D., Ochsenbein, C., Laloi, C., Kim, C., Danon, A., Wagner, D., Hideg, E., Göbel, C., Feussner, I., Nater, M., and Apel, K. (2003) Rapid induction of distinct stress responses after the release of singlet oxygen in Arabidopsis. Plant Cell 15, 2320-2332
26. Khandal, D., Samol, I., Buhr, F., Pollmann, S., Schmidt, H., Clemens, S., Reinbothe, S., and Reinbothe, C. (2009) Singlet oxygen-dependent translational control in the tigrina-d.12 mutant of barley. Proc. Natl. Acad. Sci. U.S.A. 106, 13112-13117
27. Kim, C., and Apel, K. (2013) Singlet oxygen-mediated signaling in plants: moving from flu to wild type reveals an increasing complexity. Photosynth. Res. 116, 455-464
28. Burkhard, P., Stetefeld, J., and Strelkov, S. V. (2001) Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11, 82-88
29. Czarnecki, O., Hedtke, B., Melzer, M., Rothbart, M., Richter, A., Schröter, Y., Pfannschmidt, T., and Grimm, B. (2011) An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts. Plant Cell 23, 4476-4491
30. Czarnecki, O., and Grimm, B. (2013) New insights in the topology of the biosynthesis of 5-aminolevulinic acid. Plant Signal. Behav. 8, e23124
31. DeLano, W. L. (2010) The PyMOL Molecular Graphics System, version 1.3r1, Schrödinger, LLC, New York