Abstract
Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Zα. Here we report the solution structure of free Zα and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Zα) 2 /Z-DNA complex shows that most Z-DNA contacting residues in free Zα are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (α+β)helix–turn–helix/B-DNA complexes suggests that binding of Zα to B-DNA is disfavored by steric hindrance, but does not eliminate the possibility that related domains may bind to both B- and Z-DNA.
Bibliography
Schade, M., Turner, C. J., Kühne, R., Schmieder, P., Lowenhaupt, K., Herbert, A., Rich, A., & Oschkinat, H. (1999). The solution structure of the Zα domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA. Proceedings of the National Academy of Sciences, 96(22), 12465â12470.
References
26
Referenced
79
-
B Sommer, M Kohler, R Sprengel, P H Seeburg Cell 67, 11–19 (1991).
(
10.1016/0092-8674(91)90568-J
) / Cell by Sommer B (1991) -
C M Burns, H Chu, S M Rueter, L K Hutchinson, H Canton, E Sanders-Bush, R Emeson Nature (London) 387, 303–308 (1997).
(
10.1038/387303a0
) / Nature (London) by Burns C M (1997) -
A G Polson, B L Bass EMBO J 13, 5701–5711 (1994).
(
10.1002/j.1460-2075.1994.tb06908.x
) / EMBO J by Polson A G (1994) -
A Herbert, J Alfken, Y G Kim, S Mian, K Nishikura, A Rich Proc Natl Acad Sci USA 94, 8421–8426 (1997).
(
10.1073/pnas.94.16.8421
) / Proc Natl Acad Sci USA by Herbert A (1997) -
A Herbert, A Rich J Biol Chem 271, 11595–11598 (1996).
(
10.1074/jbc.271.20.11595
) / J Biol Chem by Herbert A (1996) -
M Schade, J Behlke, K Lowenhaupt, A Herbert, A Rich, H Oschkinat FEBS Lett 458, 27–36 (1999).
(
10.1016/S0014-5793(99)01119-9
) / FEBS Lett by Schade M (1999) -
T Schwartz, M A Rould, K Lowenhaupt, A Herbert, A Rich Science 284, 1841–1845 (1999).
(
10.1126/science.284.5421.1841
) / Science by Schwartz T (1999) -
M Schade, C J Turner, K Lowenhaupt, A Rich, A Herbert EMBO J 18, 470–479 (1999).
(
10.1093/emboj/18.2.470
) / EMBO J by Schade M (1999) -
A Herbert, M Schade, K Lowenhaupt, J Alfken, T Schwartz, L S Shlyakhtenko, Z L Lyubchenko, A Rich Nucleic Acids Res 26, 3486–3493 (1998).
(
10.1093/nar/26.15.3486
) / Nucleic Acids Res by Herbert A (1998) -
I Berger, W Winston, R Manoharan, T Schwartz, J Alfken, Y G Kim, K Lowenhaupt, A Herbert, A Rich Biochemistry 37, 13313–13321 (1998).
(
10.1021/bi9813126
) / Biochemistry by Berger I (1998) - J Cavanagh, W J Fairbrother, A G Palmer, N J Skelton Protein NMR Spectroscopy (Academic, San Diego, 1996). / Protein NMR Spectroscopy by Cavanagh J (1996)
-
W G Vuister, A Bax J Am Chem Soc 115, 7772–7777 (1993).
(
10.1021/ja00070a024
) / J Am Chem Soc by Vuister W G (1993) -
F Delaglio, S Grzesiek, G Vuister, G Zhu, J Pfeifer, A Bax J Biomol NMR 6, 277–293 (1995).
(
10.1007/BF00197809
) / J Biomol NMR by Delaglio F (1995) -
J L Markley, A Bax, Y Arata, C W Hilbers, R Kapein, B D Sykes, P E Wright, K Wuthrich J Mol Biol 280, 933–952 (1998).
(
10.1006/jmbi.1998.1852
) / J Mol Biol by Markley J L (1998) -
J Kuszewski, M Nilges, A T Brunger J Biomol NMR 2, 33–56 (1992).
(
10.1007/BF02192799
) / J Biomol NMR by Kuszewski J (1992) - A T Brünger x-plor, Version 3.1: A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, 1993). / x-plor, Version 3.1: A System for X-ray Crystallography and NMR by Brünger A T (1993)
-
M P Foster, D S Wuttke, K R Clemens, W Jahnke, I Radhakrishnan, L Tennant, M Reymond, J Chung, P E Wright J Biomol NMR 12, 51–71 (1998).
(
10.1023/A:1008290631575
) / J Biomol NMR by Foster M P (1998) -
M Billeter, P Guntert, P Luginbuhl, K Wuthrich Cell 85, 1057–1065 (1996).
(
10.1016/S0092-8674(00)81306-9
) / Cell by Billeter M (1996) -
J A Hirsch, A K Aggarwal EMBO J 14, 6280–6291 (1995).
(
10.1002/j.1460-2075.1995.tb00318.x
) / EMBO J by Hirsch J A (1995) -
S E Ades, R T Sauer Biochemistry 33, 9187–9194 (1994).
(
10.1021/bi00197a022
) / Biochemistry by Ades S E (1994) -
L Holm, C Sander Science 273, 595–602 (1996).
(
10.1126/science.273.5275.595
) / Science by Holm L (1996) -
A White, X Ding, J C vanderSpek, J R Murphy, D Ringe Nature (London) 394, 502–506 (1998).
(
10.1038/28893
) / Nature (London) by White A (1998) -
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) -
S C Schulz, G C Shields, T A Steitz Science 253, 1001–1007 (1991).
(
10.1126/science.1653449
) / Science by Schulz S C (1991) -
N Zheng, E Fraenkel, C O Pabo, N P Pavletich Genes Dev 13, 666–674 (1999).
(
10.1101/gad.13.6.666
) / Genes Dev by Zheng N (1999) -
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, 1 month ago (July 26, 2002, 10:35 a.m.) |
Deposited | 3 years, 2 months ago (June 7, 2022, 12:17 a.m.) |
Indexed | 2 months, 3 weeks ago (June 6, 2025, 6:44 a.m.) |
Issued | 25 years, 10 months ago (Oct. 26, 1999) |
Published | 25 years, 10 months ago (Oct. 26, 1999) |
Published Online | 25 years, 10 months ago (Oct. 26, 1999) |
Published Print | 25 years, 10 months ago (Oct. 26, 1999) |
@article{Schade_1999, title={The solution structure of the Zα domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.22.12465}, DOI={10.1073/pnas.96.22.12465}, number={22}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Schade, Markus and Turner, Christopher J. and Kühne, Ronald and Schmieder, Peter and Lowenhaupt, Ky and Herbert, Alan and Rich, Alexander and Oschkinat, Hartmut}, year={1999}, month=oct, pages={12465–12470} }