DNA Recognition by Cys2His2 Zinc Finger Proteins

Annual Reviews - Tập 29 Số 1 - Trang 183-212 - 2000
Scot A. Wolfe1, Lena Nekludova1, Carl O. Pabo1
1Department of Biology, 68-580, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139;

Tóm tắt

▪ Abstract  Cys2His2 zinc fingers are one of the most common DNA-binding motifs found in eukaryotic transcription factors. These proteins typically contain several fingers that make tandem contacts along the DNA. Each finger has a conserved ββα structure, and amino acids on the surface of the α-helix contact bases in the major groove. This simple, modular structure of zinc finger proteins, and the wide variety of DNA sequences they can recognize, make them an attractive framework for attempts to design novel DNA-binding proteins. Several studies have selected fingers with new specificities, and there clearly are recurring patterns in the observed side chain–base interactions. However, the structural details of recognition are intricate enough that there are no general rules (a “recognition code”) that would allow the design of an optimal protein for any desired target site. Construction of multifinger proteins is also complicated by interactions between neighboring fingers and the effect of the intervening linker. This review analyzes DNA recognition by Cys2His2 zinc fingers and summarizes progress in generating proteins with novel specificities from fingers selected by phage display.

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Tài liệu tham khảo

10.1016/S0378-1119(98)00213-3

10.1093/nar/21.18.4218

10.1002/pro.5560070103

10.1093/nar/26.7.1784

10.1101/gad.8.14.1664

10.1002/prot.340080405

10.1073/pnas.95.25.14628

10.1073/pnas.88.9.3608

10.1146/annurev.biophys.26.1.357

10.1126/science.271.5252.1081

10.1074/jbc.273.33.21246

10.1093/nar/25.12.2464

10.1038/8283

10.1016/0014-5793(85)80723-7

10.1073/pnas.93.15.7562

10.1006/jmbi.1997.1339

10.1093/nar/21.15.3341

10.1073/pnas.91.23.11168

10.1073/pnas.91.23.11163

10.1016/S0959-440X(97)80015-2

10.1038/372642a0

10.1126/science.282.5396.2018

10.1006/jmbi.1994.1701

10.1146/annurev.bi.61.070192.004341

Cook WJ, 1994, J. Biol. Chem., 269, 9374, 10.1016/S0021-9258(17)37118-1

10.1006/bbrc.1998.9850

10.1016/S0014-5793(97)01257-X

Crozatier M, 1992, Genetics, 131, 905, 10.1093/genetics/131.4.905

Davies R, 1999, Cancer Res., 59, S1747

10.1002/prot.340120202

10.1073/pnas.89.16.7345

10.1073/pnas.90.6.2256

10.1073/pnas.91.23.11099

10.1016/S0969-2126(96)00064-0

10.1016/S0969-2126(98)00047-1

10.1074/jbc.274.27.19281

10.1016/S0969-2126(96)00125-6

10.1016/S0092-8674(80)80048-1

10.1073/pnas.92.26.11960

10.1016/0022-2836(92)90952-G

10.1038/366483a0

10.1006/jmbi.1997.1177

10.1021/bi9825293

10.1038/nsb0897-605

10.1073/pnas.84.14.4841

10.1073/pnas.86.12.4599

10.1093/nar/21.13.3117

10.1042/bj3330085

10.1182/blood.V87.5.1793.1793

10.1126/science.275.5300.657

10.1074/jbc.271.21.12431

10.1021/bi9717993

Hanas JS, 1983, J. Biol. Chem., 258, 14120, 10.1016/S0021-9258(17)43831-2

10.1016/0888-7543(92)90372-Y

10.1073/pnas.93.24.13577

10.1021/bi981358z

10.1002/j.1460-2075.1992.tb05552.x

10.1021/bi00185a004

10.1073/pnas.93.23.12834

10.1021/bi9811112

10.1006/jmbi.1994.0468

10.1038/nsb1196-940

10.1073/pnas.94.8.3616

10.1074/jbc.272.47.29795

10.1073/pnas.95.6.2812

10.1073/pnas.93.3.1156

10.1016/S0378-1119(97)00489-7

10.1101/gad.10.1.27

10.1016/0167-4781(94)90128-7

10.1096/fasebj.9.8.7768350

10.1073/pnas.86.16.6097

10.1002/j.1460-2075.1991.tb07861.x

10.1021/ja00012a021

10.1021/ic00058a030

10.1016/S1357-2725(97)00094-0

10.1016/0092-8674(95)90392-5

10.1073/pnas.90.13.6145

10.1126/science.2503871

10.1073/pnas.94.11.5525

Losson R, 1997, Biol. Chem., 378, 579

10.1016/S0968-0004(97)01168-7

10.1128/MCB.15.5.2437

10.1021/ja00014a045

10.1073/pnas.89.11.4796

10.1002/j.1460-2075.1985.tb03825.x

10.1016/S0167-4838(98)00015-6

10.1093/nar/20.16.4137

10.1038/349175a0

10.1073/pnas.91.15.6948

10.1016/0022-2836(92)90846-C

10.1073/pnas.95.6.2938

10.1038/nsb0297-122

Pabo CO, Nekludova L. 2000. Geometric analysis and comparisonj of protein-DNA interfaces: Why is there no simple code for recognition? Submitted

10.1016/0092-8674(87)90595-2

10.1126/science.3047872

10.1126/science.2028256

10.1126/science.8378770

10.1128/MCB.14.10.6570

10.1073/pnas.92.21.9752

10.1126/science.7809612

10.1021/bi972464o

10.1021/tx00050a005

Ptashne M, 1992, A Genetic Switch.

Rebar EJ. 1997. Selection studies of zinc finger–DNA recognition. PhD thesis. MIT, Cambridge, MA

10.1126/science.8303274

Richardson JS, Richardson DC. 1989. InPrinciples and Patterns of Protein Conformation, ed. GD Fasman, pp. 1–98. New York: Plenum

10.1038/nm0996-1028

10.1093/nar/26.3.703

10.1093/nar/19.8.1797

10.1016/0959-4388(95)80060-3

10.1073/pnas.96.6.2758

Shastry BS, 1996, J. Cell. Sci., 109, 535, 10.1242/jcs.109.3.535

Shi Y. 1995. Molecular mechanisms of zinc finger protein-nucleic acid interactions. PhD thesis. John Hopkins Univ., Baltimore, MD

10.1016/1074-5521(95)90280-5

10.1021/bi952384p

10.1093/nar/26.3.796

10.1126/science.4001944

10.1093/nar/22.16.3397

10.1128/MCB.15.4.2275

10.1007/s000180050186

10.1073/pnas.88.20.9188

10.1128/MCB.12.6.2784

10.1073/pnas.96.17.9568

10.1021/bi00494a008

10.1006/jmbi.1998.2421

10.1073/pnas.92.2.344

10.1006/jmbi.1997.1291

10.1126/science.283.5398.88

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Annual Reviews

Tập 29 Số 1

183-212

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