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Structure of the POU Domain

  • Chapter
Mechanisms of Transcription

Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC,volume 11))

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Abstract

A recurring motif in molecular biology is the presence of families of molecular structures that serve similar functions in the cell. This is particularly true for proteins regulating DNA transcription, i.e. the transcription factors. Up till now, a number of different transcription factor families have been classified, each of which is characterized by the presence of a structurally conserved region where the DNA-binding ability of the protein resides (reviewed in Pabo and Sauer 1992). Examples of this are the zinc-finger proteins, leucine zippers and helix-turn-helix (HTH) proteins.

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References

  • Assa-Munt N, Mortishire-Smith RJ, Aurora R, Herr W, Wright PE (1993) The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage λ repressor DNA-binding domain. Cell 73:193–205

    Article  PubMed  CAS  Google Scholar 

  • Billeter M, Qian YQ, Otting G, Müller M, Gehring W, Wüthrich K (1993) Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J Mol Biol 234:1084–1097

    Article  PubMed  CAS  Google Scholar 

  • Bodner M, Castrillo JL, Theill LE, Deerinck T, Ellisman M, Karin M (1988) The pituitary-specific transcription factor GHF-1 is a homeobox-containing protein. Cell 55:505–518

    Article  PubMed  CAS  Google Scholar 

  • Botfield MC, Weiss MA (1994) Bipartite DNA recognition by the human Oct-2 POU domain: POUs-specific phosphate contacts are analogous to those of bacteriophage λ repressor. Biochemistry 33:2349–2355

    Article  PubMed  CAS  Google Scholar 

  • Botfield MC, Jancso A, Weiss MA (1992) Biochemical characterization of the Oct-2 POU domain with implications for bipartite DNA recognition. Biochemistry 31:5841–5848

    Article  PubMed  CAS  Google Scholar 

  • Churchill MEA, Tullius TD, Klug A (1990) Mode of interaction of the zinc-finger protein TFIIIA with a 5SRNA gene of Xenopus. Proc Natl Acad Sci USA 87: 5528–5532

    Article  PubMed  CAS  Google Scholar 

  • Clark KL, Halay ED, Lai E, Burley SK (1993) Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 364:412–420

    Article  PubMed  CAS  Google Scholar 

  • Clerc RG, Corcoran LM, LeBowitz JH, Baltimore D, Sharp PA (1988) The B- cell-specific Oct-2 protein contains POU box- and homeo box-type domains. Genes Dev 2:1570–1581

    Article  PubMed  CAS  Google Scholar 

  • Cox MM (1995) The subdomains of the POU-domain: structure determination by NMR. Doctoral Diss, Utrecht University, Utrecht

    Google Scholar 

  • Cox MM, Dekker N, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R (1993) NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential lH and l3N assignments and secondary structure. Biochemistry 32:6032–6040

    Article  PubMed  CAS  Google Scholar 

  • Cox MM, van Tilborg PJA, de Laat W, Boelens R, van Leeuwen HC, van der Vliet PC, Kaptein R (1995) Solution structure of the Oct-1 POU-homeodomain determined by NMR and restrained molecular dynamics. J Biomol NMR 6:23–32

    Google Scholar 

  • Dekker N, Cox MM, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R (1993) Solution structure of the POU-specific DNA-binding domain of Oct-1. Nature 362:852–854

    Article  PubMed  CAS  Google Scholar 

  • Finney M, Ruvkun G, Horvitz HR (1988) The C. elegans cell lineage and differentiation gene unc-86 encodes a protein with a homeodomain and extended similarity to transcription factors. Cell 55:757–769

    Article  PubMed  CAS  Google Scholar 

  • Fogh RH, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R (1994) Solution structure of the LexA repressor DNA binding domain determined by lH NMR spectroscopy. EMBO J 13:3936–3944

    PubMed  CAS  Google Scholar 

  • Gehring WJ, Affolter M, Bürglin T (1994) Homeodomain proteins. Annu Rev Biochem 63:487–526

    Article  PubMed  CAS  Google Scholar 

  • Herr W, Cleary MA (1995) The POU domain: versatility in transcriptional regulation by a flexible two-in-one DNA-binding domain. Genes Dev 9:1679–1693

    Article  PubMed  CAS  Google Scholar 

  • Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233:123–138

    Article  PubMed  CAS  Google Scholar 

  • Ingraham HA, Chen R, Mangalam HJ, Elsholtz HP, Flynn SE, Lin CR, Simmons DM, Swanson L, Rosenfeld MG (1988) A tissue-specific transcription factor containing a homeodomain specifies a pituitary phenotype. Cell 55:519–529

    Article  PubMed  CAS  Google Scholar 

  • Kissinger CR, Liu B, Martin-Blanco E, Kornberg TB, Pabo CO (1990) Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Ä resolution: a framework for understanding homeodomain-DNA interactions. Cell 63:579–590

    Article  PubMed  CAS  Google Scholar 

  • Klemm JD, Pabo CO (1996) Oct-1 POU domain-DNA interactions: the cooperative binding of isolated subdomains and effects of covalent linkage. Genes Dev 10:27–36

    Article  Google Scholar 

  • Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO (1994) Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77:21–32

    Article  PubMed  CAS  Google Scholar 

  • Ko HS, Fast P, McBride W, Staudt LM (1988) A human protein specific for the immunoglobulin octamer DNA motif contains a functional homeobox domain. Cell 55:135–144

    Article  PubMed  CAS  Google Scholar 

  • Kraulis P (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946–950

    Article  Google Scholar 

  • Li P, He X, Gerrero MR, Mok M, Aggarwal A, Rosenfeld MG (1993) Spacing and orientation of bipartite DNA-binding motifs as potential functional determinants for POU domain factors. Genes Dev 7:2483–2496

    Article  PubMed  CAS  Google Scholar 

  • Morita EH, Shirakawa M, Hayashi F, Imagawa M, Kyogoku Y (1993) Secondary structure of the Oct-3 POU homeodomain as determined by 1H-15N NMR spectroscopy. FEBS Lett 321:107–110

    Article  PubMed  CAS  Google Scholar 

  • Müller MM, Ruppert S, Schaffner W, Matthias P (1988) A cloned octamer transcription factor stimulates transcription from lymphoid-specific promoters in non-B cells. Nature 336:544–551

    Article  PubMed  Google Scholar 

  • Nardelli J, Gibson TJ, Vesque C, Charnay P (1990) Base sequence discrimination by zinc-finger DNA-binding domains. Nature 349:175–178

    Article  Google Scholar 

  • Ogata K, Hojo H, Aimoto S, Nakai T, Nakamura H, Sarai A, Ishii S, Nishimura Y (1992) Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core. Proc Natl Acad Sci USA 89:6428–6432

    Article  PubMed  CAS  Google Scholar 

  • Otting G, Qian Y, Müller M, Gehring WJ, Wüthrich K (1988) Secondary structure determination for the Antennapedia homeodomain by nuclear magnetic resonance and evidence for a helix-turn-helix motif EMBO J 7:4305–4309

    PubMed  CAS  Google Scholar 

  • Otting G, Qian YQ, Billeter M, Müller M, Affolter M, Gehring WJ, Wüthrich K (1990) Protein-DNA contacts in the structure of a homeodomain-DNA complex by nuclear magnetic resonance spectroscopy in solution. EMBO J 9:3085–3092

    PubMed  CAS  Google Scholar 

  • Pabo CO, Sauer RT (1992) Transcription factors: structural families and principles of DNA recognition. Annu Rev Biochem 61:1053–1095

    Article  PubMed  CAS  Google Scholar 

  • Pavletich NP, Pabo CO (1991) Zinc-finger DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Ã…. Science 252:809–817

    Article  PubMed  CAS  Google Scholar 

  • Qian YQ, Billeter M, Otting G, Müller M, Gehring WJ, Wüthrich K (1988) The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors. Cell 59:573–580

    Article  Google Scholar 

  • Qian YQ, Otting G, Billeter M, Müller M, Gehring W, Wüthrich K (1993) Nuclear magnetic resonance spectroscopy of a DNA complex with the uniformlyl 13C-labeled Antennapedia homeodomain and structure determination of the DNA-bound homeodomain. J Mol Biol 234:1070–1083

    Article  PubMed  CAS  Google Scholar 

  • Qian YQ, Furukubo-Tokunaga K, Resendez-Perez D, Müller M, Gehring WJ, Wüthrich K (1994) Nuclear magnetic resonance solution structure of the fushi tarazu homeodomain from Drosophila and comparison with the Antennapedia homeodomain. J Mol Biol 238:33–345

    Article  Google Scholar 

  • Ramakrishnan V, Finch JT, Graziano V, Lee PL, Sweet RM (1993) Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362:219–223

    Article  PubMed  CAS  Google Scholar 

  • Rosenfeld MG (1991) POU domain transcription factors: pou-er-ful developmental regulators. Genes Dev 5:897–907

    Article  PubMed  CAS  Google Scholar 

  • Ruvkun G, Finney M (1991) Regulation of transcription and cell identity by POU domain proteins. Cell 64:475–478

    Article  PubMed  CAS  Google Scholar 

  • Schaffner W (1989) How do different transcription factors binding the same DNA sequence sort out their jobs? Trends Genet 5:37–39

    Article  PubMed  CAS  Google Scholar 

  • Scheidereit C, Cromlish JA, Gerster T, Kawakami K, Balmaceda CG, Currie AR, Roeder RG (1988) A human lymphoid-specific transcription factor that activates immunoglobulin genes is a homeobox protein. Nature 336:551–557

    Article  PubMed  CAS  Google Scholar 

  • Schöler HR (1991) Octamania: the POU factors in murine development. Trends Genet 7:323–329

    PubMed  Google Scholar 

  • Segil N, Roberts SB, Heintz N (1991) Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 DNA binding activity. Science 254:1814–1816

    Article  PubMed  CAS  Google Scholar 

  • Sivaraja M, Botfield MC, Mueller M, Jancso A, Weiss MA (1994) Solution structure of a POU-specific homeodomain: 3D-NMR studies of human B-cell transcription factor Oct-2. Biochemistry 3:9845–9855

    Article  Google Scholar 

  • Sturm RA, Herr W (1988) The POU domain is a bipartite DNA-binding structure. Nature 336:601–604

    Article  PubMed  CAS  Google Scholar 

  • Sturm RA, Das G, Herr W (1988) The ubiquitous octamer-binding protein Oct-1 contains a POU domain with a homeo box subdomain. Genes Dev 2:1582–1599

    Article  PubMed  CAS  Google Scholar 

  • Verrijzer CP, Oosterhout JA, van Weperen WW, van der Vliet PC (1991) POU proteins bend DNA via the POU-specific domain. EMBO J 10:3007–3014

    PubMed  CAS  Google Scholar 

  • Verrijzer CP, Alkema MJ, van Weperen WW, van Leeuwen HC, Strating MJJ, van der Vliet PC (1992) The DNA-binding specificity of the bipartite POU domain and its subdomains. EMBO J 11:4993–5003

    PubMed  CAS  Google Scholar 

  • Wey E, Lyons GE, Schäfer BW (1994) A human POU domain gene, mPOU, is expressed in developing brain and specific abult tissues. Eur J Bioch 220:753–762

    Google Scholar 

  • Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO (1991) Crystal structure of MATα2 homeodomain-operator complex suggests a general model for homeodomain DNA interactions. Cell 67:517–528

    Article  PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands

    M. M. Cox, R. Boelens & R. Kaptein

  2. Laboratory of Physiological Chemistry, Utrecht University, Stratenum, P.O. Box 80042, 3508 TA, Utrecht, The Netherlands

    P. C. Van der Vliet

Authors
  1. M. M. Cox
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  2. R. Boelens
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  3. P. C. Van der Vliet
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  4. R. Kaptein
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Editor information

Editors and Affiliations

  1. Max-Planck-Institut für Experimentelle Medizin, Hermann-Rein-Straße 3, 37075, Göttingen, Germany

    Fritz Eckstein

  2. Biochemistry Department, University of Dundee, DD1 4HN, Dundee, UK

    David M. J. Lilley

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© 1997 Springer-Verlag Berlin Heidelberg

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Cox, M.M., Boelens, R., Van der Vliet, P.C., Kaptein, R. (1997). Structure of the POU Domain. In: Eckstein, F., Lilley, D.M.J. (eds) Mechanisms of Transcription. Nucleic Acids and Molecular Biology, vol 11. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60691-5_15

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  • DOI: https://doi.org/10.1007/978-3-642-60691-5_15

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-64509-9

  • Online ISBN: 978-3-642-60691-5

  • eBook Packages: Springer Book Archive

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