Abstract
The three-dimensional structure of the human Rap30 DNA-binding domain has been solved by multinuclear NMR spectroscopy. The structure of the globular domain is strikingly similar to that of linker histone H5 and its fold places Rap30 into the “winged” helix–turn–helix family of eukaryotic transcription factors. Although the domain interacts weakly with DNA, the binding surface was identified and shown to be consistent with the structure of the HNF-3/ fork head –DNA complex. The architecture of the Rap30 DNA-binding domain has important implications for the function of Rap30 in the assembly of the preinitiation complex. In analogy to the function of linker histones in chromatin formation, the fold of the Rap30 DNA-binding domain suggests that its role in transcription initiation may be that of a condensation factor for preinitiation complex assembly. Functional similarity to linker histones may explain the dependence of Rap30 binding on the bent DNA environment induced by the TATA box-binding protein. Cryptic sequence identity and functional homology between the Rap30 DNA-binding domain and region 4 of Escherichia coli σ 70 may indicate that the σ factors also possess a linker histone-like activity in the formation of a prokaryotic closed complex.
References
50
Referenced
59
-
R G Roeder Trends Biochem Sci 21, 327–335 (1996).
(
10.1016/0968-0004(96)10050-5
) / Trends Biochem Sci by Roeder R G (1996) -
L Zawel, D Reinberg Annu Rev Biochem 64, 533–561 (1995).
(
10.1146/annurev.bi.64.070195.002533
) / Annu Rev Biochem by Zawel L (1995) -
D Reines, J W Conaway, R C Conaway Trends Biochem Sci 21, 351–355 (1996).
(
10.1016/0968-0004(96)10045-1
) / Trends Biochem Sci by Reines D (1996) -
L Zawel, D Reinberg Prog Nucleic Acids Res Mol Biol 44, 67–108 (1993).
(
10.1016/S0079-6603(08)60217-2
) / Prog Nucleic Acids Res Mol Biol by Zawel L (1993) -
S Tan, T Aso, R C Conaway, J W Conaway J Biol Chem 269, 25684–25691 (1994).
(
10.1016/S0021-9258(18)47303-6
) / J Biol Chem by Tan S (1994) -
F-W Sun, M Hempsey Proc Natl Acad Sci USA 92, 3127–3131 (1995).
(
10.1073/pnas.92.8.3127
) / Proc Natl Acad Sci USA by Sun F-W (1995) -
S M Fang, Z F Burton J Biol Chem 271, 11703–11709 (1996).
(
10.1074/jbc.271.20.11703
) / J Biol Chem by Fang S M (1996) - C A Gross, M Lonetto, R Losick Transcriptional Regulation, eds S L McKnight, K R Yamamoto (Cold Spring Harbor Lab. Press, Plainview, NY), pp. 129–176 (1994). / Transcriptional Regulation by Gross C A (1994)
-
S Tan, K P Garrett, R C Conaway, J W Conaway Proc Natl Acad Sci USA 91, 9808–9812 (1994).
(
10.1073/pnas.91.21.9808
) / Proc Natl Acad Sci USA by Tan S (1994) -
S Tan, R C Conaway, J W Conaway Proc Natl Acad Sci USA 92, 6042–6046 (1995).
(
10.1073/pnas.92.13.6042
) / Proc Natl Acad Sci USA by Tan S (1995) -
T Gardella, T Moyle, M M Susskind J Mol Biol 206, 579–590 (1989).
(
10.1016/0022-2836(89)90567-6
) / J Mol Biol by Gardella T (1989) -
D A Siegele, J C Hu, W A Walter, C A Gross J Mol Biol 206, 591–603 (1989).
(
10.1016/0022-2836(89)90568-8
) / J Mol Biol by Siegele D A (1989) -
S McCracken, J Greenblatt Science 253, 900–902 (1991).
(
10.1126/science.1652156
) / Science by McCracken S (1991) -
V Ramakrishnan, J T Finch, V Graziano, P L Lee, R M Sweet Nature (London) 362, 219–223 (1993).
(
10.1038/362219a0
) / Nature (London) by Ramakrishnan V (1993) -
K L Clark, E D Halay, E Lai, S K Burley Nature (London) 364, 412–420 (1993).
(
10.1038/364412a0
) / Nature (London) by Clark K L (1993) -
A Bax, S Grzesiek Acc Chem Res 26, 131–138 (1993).
(
10.1021/ar00028a001
) / Acc Chem Res by Bax A (1993) -
G M Clore, A M Gronenborn Science 252, 1390–1399 (1991).
(
10.1126/science.2047852
) / Science by Clore G M (1991) -
G M Clore, A M Gronenborn Protein Sci 3, 372–390 (1994).
(
10.1002/pro.5560030302
) / Protein Sci by Clore G M (1994) -
A Bax, G W Vuister, S Grzesiek, F Delaglio, A C Wang, R Tschudin, G Zhu Methods Enzymol 239, 79–106 (1994).
(
10.1016/S0076-6879(94)39004-5
) / Methods Enzymol by Bax A (1994) -
M H Werner, M E Bianchi, A M Gronenborn, G M Clore Biochemistry 34, 11998–12004 (1995).
(
10.1021/bi00037a042
) / Biochemistry by Werner M H (1995) -
M A Nilges Proteins Struct Funct Genet 17, 297–309 (1993).
(
10.1002/prot.340170307
) / Proteins Struct Funct Genet by Nilges M A (1993) -
M A Nilges, G M Clore, A M Gronenborn Biopolymers 29, 813–822 (1990).
(
10.1002/bip.360290415
) / Biopolymers by Nilges M A (1990) -
M A Nilges, G M Clore, A M Gronenborn FEBS Lett 229, 317–324 (1988).
(
10.1016/0014-5793(88)81148-7
) / FEBS Lett by Nilges M A (1988) - A T Brünger X-PLOR Version 3.1: A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, CT, 1993). / X-PLOR Version 3.1: A System for X-ray Crystallography and NMR by Brünger A T (1993)
-
D S Garrett, J Kuszewski, T J Hancock, P J Lodi, G W Vuister, A M Gronenborn, G M Clore J Magn Reson Ser B 104, 99–103 (1994).
(
10.1006/jmrb.1994.1061
) / J Magn Reson Ser B by Garrett D S (1994) -
J Kuszewski, J Qin, A M Gronenborn, G M Clore J Magn Reson Ser B 106, 92–96 (1995).
(
10.1006/jmrb.1995.1017
) / J Magn Reson Ser B by Kuszewski J (1995) -
J Kuszewski, A M Gronenborn, G M Clore J Magn Reson 125, 171–177 (1997).
(
10.1006/jmre.1997.1116
) / J Magn Reson by Kuszewski J (1997) -
K P Wilson, L M Shewchuk, R G Brenan, A J Otsuka, B W Matthews Proc Natl Acad Sci USA 89, 9257–9261 (1992).
(
10.1073/pnas.89.19.9257
) / Proc Natl Acad Sci USA by Wilson K P (1992) -
R H Fogh, G Ottleben, H Ruterjans, M Schnarr, R Boelens, R Kaptein EMBO J 13, 3936–3944 (1994).
(
10.1002/j.1460-2075.1994.tb06709.x
) / EMBO J by Fogh R H (1994) -
C O Pabo, R T Sauer Annu Rev Biochem 61, 1053–1095 (1992).
(
10.1146/annurev.bi.61.070192.005201
) / Annu Rev Biochem by Pabo C O (1992) -
K Ogata, H Hojo, S Aimoto, T Nakai, H Nakamura, A Sarai, S Ishii, Y Nishimura Proc Natl Acad Sci USA 89, 6428–6432 (1992).
(
10.1073/pnas.89.14.6428
) / Proc Natl Acad Sci USA by Ogata K (1992) -
R Kodandapani, F Pio, C Z Ni, G Piccialli, M Klemsz, S McKercher, R A Maki, K R Ely Nature (London) 380, 456–460 (1996).
(
10.1038/380456a0
) / Nature (London) by Kodandapani R (1996) -
M H Werner, G M Clore, C L Fisher, R J Fisher, L Trinh, J Shiloach, A M Gronenborn J Biomol NMR 10, 317–328 (1997).
(
10.1023/A:1018399711996
) / J Biomol NMR by Werner M H (1997) -
A Batchelor, D E Piper, F C dela Brousse, S L McKnight, C Wolberger Science 279, 1037–1041 (1998).
(
10.1126/science.279.5353.1037
) / Science by Batchelor A (1998) -
N Assa-Munt, R J Mortishire-Smith, R Aurora, W Herr, P E Wright Cell 73, 193–205 (1993).
(
10.1016/0092-8674(93)90171-L
) / Cell by Assa-Munt N (1993) -
F Robert, D Forget, J Li, J Greenblatt, B Coulombe J Biol Chem 271, 8517–8520 (1996).
(
10.1074/jbc.271.15.8517
) / J Biol Chem by Robert F (1996) -
B Q Wang, C F Kostrub, A Finkelstein, Z F Burton Protein Expression Purif 4, 207–214 (1993).
(
10.1006/prep.1993.1027
) / Protein Expression Purif by Wang B Q (1993) -
G Felsenfeld, J Boyes, J Chung, D Clark, V Studitsky Proc Natl Acad Sci USA 93, 9384–9388 (1996).
(
10.1073/pnas.93.18.9384
) / Proc Natl Acad Sci USA by Felsenfeld G (1996) -
X Xie, T Kokubo, S L Cohen, A Hoffmann, B T Chait, R G Roeder, Y Nakatani, S K Burley Nature (London) 380, 316–322 (1996).
(
10.1038/380316a0
) / Nature (London) by Xie X (1996) -
F A Goytisolo, S E Gerchman, X Yu, C Rees, V Graziano, V Ramakrishnan, J O Thomas EMBO J 15, 3421–3429 (1996).
(
10.1002/j.1460-2075.1996.tb00708.x
) / EMBO J by Goytisolo F A (1996) -
J J Hayes, R Kaplan, K Ura, D Pruss, A Wolffe J Biol Chem 271, 25817–25822 (1996).
(
10.1074/jbc.271.42.25817
) / J Biol Chem by Hayes J J (1996) -
L A Cirillo, C E McPherson, P Bossard, K Stevens, S Cherian, E Y Shim, K L Clark, S K Burley, K S Zaret EMBO J 17, 244–254 (1998).
(
10.1093/emboj/17.1.244
) / EMBO J by Cirillo L A (1998) -
D Pruss, B Bartholomew, J Persinger, J Hayes, G Arents, E N Moudrianakis, A P Wolffe Science 274, 614–617 (1996).
(
10.1126/science.274.5287.614
) / Science by Pruss D (1996) -
D Forget, F Robet, G Grondin, Z F Burton, J Greenblatt, B Coulombe Proc Natl Acad Sci USA 94, 7150–7155 (1997).
(
10.1073/pnas.94.14.7150
) / Proc Natl Acad Sci USA by Forget D (1997) -
T-Y Kim, T Lagrane, Y-H Wang, J D Griffith, D Reinberg, R H Ebright Proc Natl Acad Sci USA 94, 12268–12273 (1997).
(
10.1073/pnas.94.23.12268
) / Proc Natl Acad Sci USA by Kim T-Y (1997) -
O Flores, I Ha, D Reinberg J Biol Chem 265, 5629–5634 (1990).
(
10.1016/S0021-9258(19)39408-6
) / J Biol Chem by Flores O (1990) -
S Buratowski, M Sopta, J Greenblatt, P A Sharp Proc Natl Acad Sci USA 88, 7509–7513 (1991).
(
10.1073/pnas.88.17.7509
) / Proc Natl Acad Sci USA by Buratowski S (1991) -
M Sopta, A F Burton, J Greenblatt Nature (London) 341, 410–414 (1989).
(
10.1038/341410a0
) / Nature (London) by Sopta M (1989) -
K P Garrett, H Serizawa, J P Hanley, J N Bradsher, A Tsuboi, N Arai, T Yokota, K-I Arai, R C Conaway, J W Conaway J Biol Chem 25, 23942–23949 (1992).
(
10.1016/S0021-9258(18)35928-3
) / J Biol Chem by Garrett K P (1992) -
R A Laskowski, M W MacArthur, D S Moss, J M Thornton J Appl Crystallogr 26, 283–291 (1993).
(
10.1107/S0021889892009944
) / J Appl Crystallogr by Laskowski R A (1993)
Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:40 a.m.) |
Deposited | 3 years, 2 months ago (June 6, 2022, 9:31 p.m.) |
Indexed | 1 year, 1 month ago (July 1, 2024, 1:12 p.m.) |
Issued | 27 years ago (Aug. 4, 1998) |
Published | 27 years ago (Aug. 4, 1998) |
Published Online | 27 years ago (Aug. 4, 1998) |
Published Print | 27 years ago (Aug. 4, 1998) |
@article{Groft_1998, title={Structural homology between the Rap30 DNA-binding domain and linker histone H5: Implications for preinitiation complex assembly}, volume={95}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.95.16.9117}, DOI={10.1073/pnas.95.16.9117}, number={16}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Groft, Caroline M. and Uljon, Sacha N. and Wang, Rong and Werner, Milton H.}, year={1998}, month=aug, pages={9117–9122} }