A basic helix-loop-helix-leucine zipper transcription complex in yeast functions in a signaling pathway from mitochondria to the nucleus

Molecular and Cellular Biology

Volumn 17, Issue 3, 1997, Pages 1110-1117

  Jia, Yankai ^a   Rothermel, Beverly ^a   Thornton, Janet ^a   Butow, Ronald A ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; LEUCINE ZIPPER PROTEIN; TRANSCRIPTION FACTOR;

ARTICLE; BINDING SITE; CELL NUCLEUS; DNA BINDING; DNA FLANKING REGION; DNA SEQUENCE; GENE EXPRESSION; GENETIC ANALYSIS; MITOCHONDRION; MOLECULAR CLONING; OPEN READING FRAME; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION;

SACCHAROMYCES CEREVISIAE;

EID: 0031027203     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.3.1110     Document Type: Article

References (43)

1. Ayer, D. E., L. Kretzner, and R. N. Eisenman. 1993. Mad: a heterodimeric partner of Max that antagonizes Myc transcriptional activity. Cell 72:211-222.
2. Benezra, R., R. L. Davis, D. Lockshon, D. L. Turner, and H. Weintraub. 1990. The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 61:49-59.
3. Blackwood, E. M., and R. N. Eisenman. 1991. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251:1211-1217.
4. Chelstowska, A. Unpublished observations.
5. Chelstowska, A., and R. A. Butow. 1995. RTG genes in yeast that function in communication between mitochondria and the nucleus are also required for expression of genes encoding peroxisomal proteins. J. Biol. Chem. 270: 18141-18146.
6. Ellenberger, T. 1994. Getting a Grip on DNA recognition - structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains. Curr. Opin. Struct. Biol. 4:12-21.
7. Ellenberger, T., D. Fass, M. Arnaud, and S. C. Harrison. 1994. Crystal structure of transcription factor E47-E-box recognition by a basic region helix-loop-helix Dimer. Genes Dev. 8:970-980.
8. Ferré-D'Amaré, A. R., G. C. Prendergast, E. B. Ziff, and S. K. Burley. 1993. Recognition by MAX of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363:38-45.
9. Fischer, D. E., L. A. Parent, and P. A. Sharp. 1993. High affinity DNA-binding Myc analogs: recognition by an α-helix. Cell 72:467-476.
10. Halazonetis, T. D., and A. N. Kandil. 1992. Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco R1. Science 255:464-466.
11. Jayaraman, P. S., K. Hirst, and C. R. Goding. 1994. The activation domain of a basic helix-loop-helix protein is masked by repressor interaction with domains distinct from that required for transcription regulation. EMBO J. 13:2192-2199.
12. Kim, J. B., G. D. Spotts, Y. D. Halvorsen, H. M. Shih, T. Ellenberger, H. C. Towle, and B. M. Spiegelman. 1995. Dual DNA binding specificity of ADD1/SREBP1 controlled by a single amino acid in the basic helix-loop-helix domain. Mol. Cell. Biol. 15:2582-2588.
13. Kim, K. S., M. S. Rosenkrantz, and L. Guarente. 1986. Saccharomyces cerevisiae contains two functional citrate synthase genes. Mol. Cell. Biol. 6: 1936-1942.
14. Kos, W., A. J. Kal, S. Vanwilpe, and H. F. Tabak. 1995. Expression of genes encoding peroxisomal proteins in Saccharomyces cerevisiae is regulated by different circuits of transcriptional control. Biochim. Biophys. Acta 1264:79-86.
15. Kunau, W.-H., A. Bühne, M. Moreno del la Garza, M. Kionka, M. Mateblowski, U. Shultz-Borchard, and R. Thieringer. 1988. Comparative enzymology of β-oxidation. Biochem. Soc. Trans. 16:418-420.
16. Lewin, A. S., V. Hines, and G. M. Small. 1990. Citrate synthase encoded by the CIT2 gene of Saccharomyces cerevisiae is peroxisomal. Mol. Cell. Biol. 10:1399-1405.
17. Liao, X., and R. A. Butow. 1993. RTG1 and RTG2: two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell 72:61-71.
18. Liao, X., W. C. Small, P. A. Srere, and R. A. Butow. 1991. Intramitochondrial functions regulate nonmitochondrial citrate synthase (CIT2) expression in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:38-46.
19. Luska, A. E., J. P. Shen, and J. P. J. Whitlock. 1993. Analysis of protein-DNA interactions at a dioxin-responsive enhancer. J. Biol. Chem. 268:6575-6580.
20. Ma, P. C. M., M. A. Rould, H. Weintraub, and C. O. Pabo. 1994. Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell 77:451-459.
21. Marshall, P. A., Y. I. Krimkevich, R. H. Lark, J. M. Dyer, M. Veenhuis, and J. M. Goodman. 1995. Pmp27 promotes peroxisomal proliferation. J. Cell Biol. 129:345-355.
22. McCammon, M. T., M. Veenhuis, S. B. Trapp, and J. M. Goodman. 1990. Association of glyoxylate and beta-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae. J. Bacteriol. 172:5816-5827.
23. Molkentin, J. D., B. L. Black, J. F. Martin, and E. N. Olson. 1995. Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins. Cell 83:1125-1136.
24. Murré. C., G. Bain, M. A. Vandijk, I. Engel, B. A. Furnari, M. E. Massari, J. R. Matthews, M. W. Quong, R. R. Rivera, and M. H. Stuiver. 1994. Structure and function of helix-loop-helix proteins. Biochim. Biophys. Acta Gene Struct. Expression 1218:129-135.
25. Murré, C., P. S. McCaw, and D. Baltimore. 1989. A new DNA-binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD and myc proteins. Cell 56:777-783.
26. Murré, C., P. S. McCaw, H. Vaessin, M. Caudy, L. Y. Jan, Y. N. Yan, C. V. Cabrera, J. N. Buskin, S. D. Hauschka, A. B. Lassar, H. Weintraub, and D. Baltimore. 1989. Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence. Cell 58:537-544.
27. Parikh, V. S., M. M. Morgan, R. Scott, L. S. Clements, and R. A. Butow. 1987. The mitochondrial genotype can influence nuclear gene expression in yeast. Science 235:576-580.
28. Pollenz, R. S., C. A. Sattler, and A. Poland. 1994. The aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator protein show distinct subcellular localizations in Hepa 1c1c7 cells by immunofluorescence microscopy. Mol. Pharmacol. 45:428-138.
29. Probst, M. R., R. V. Reisz-Porszasz, M. S. Agbunag, M. S. Ong, and O. Hankinson. 1993. Role of the aryl hydrocarbon receptor nuclear translocator protein in aryl hydrocarbon (dioxin) receptor action. Mol. Pharmacol. 44: 511-518.
30. Reyes, H., S. Reisz-Porszasz, R. V. Agbunag, M. S. Ong, and O. Hankinson. 1992. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science 256: 1193-1195.
31. Rose, M. D., P. Novick, J. H. Thomas, D. Botstein, and G. R. Fink. 1987. A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60:237-243.
32. Rose, M. D., F. Winston, and P. Heiter. 1990. Methods in yeast genetics: a laboratory course manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
33. Rothermel, B. A., A. W. Shyjan, J. L. Etheredge, and R. A. Butow. 1995. Transactivation by Rtg1p, a basic helix-loop-helix protein that functions in communication between mitochondria and the nucleus in yeast. J. Biol. Chem. 49:29476-29482.
34. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
35. Schmitt, M. E., T. A. Brown, and B. L. Trumpower. 1990. A rapid and simple method for preparation of RNA from S. cerevisiae. Nucleic Acids Res. 18:3091-3092.
36. Schreiber-Agus, N., L. Chin, K. Chen, R. Torres, G. Rao, P. Guida, A. I. Skoultchi, and R. A. DePinho. 1995. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80:777-786.
37. Shyjan, A. W., and R. A. Butow. 1993. Intracellular dialogue. Curr. Biol. 3:398-400.
38. Skoneczny, S., A. Chelstowska, and A. Rytka. 1988. Study of the coinduction by fatty acids of catalse A and acy-CoA oxidase in standard and mutant S. cerevisiae strains. Eur. J. Biochem. 174:297-302.
39. Tolbert, N. E. 1981. Metabolic pathways in peroxisomes and glyoxysomes. Annu. Rev. Biochem. 50:133-157.
40. Totonoz, P., J. B. Kim, R. A. Graves, and B. M. Speigelman. 1993. Add1: a novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation. Mol. Cell. Biol. 13:4753-4759.
41. Veenhuis, M., M. Mateblowski, W. Kunau, and W. Harder. 1987. Proliferation of microbodies in Saccharomyces cerevisiae. Yeast 3:77-84.
42. Whitelaw, M., I. Pongrantz, A. Wilhelmsson, J. A. Gustafsson, and L. Poellinger. 1993. Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. Mol. Cell. Biol. 13:2504-2514.
43. Yokoyama, C., X. Wang, M. R. Briggs, A. Admon, J. Wu, X. Hua, J. L. Goldstein, and M. S. Brown. 1993. SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene. Cell 75:187-197.