Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex

被引：105

作者：

Jin, CW ^{[1
]}

Marsden, I ^{[1
]}

Chen, XQ ^{[1
]}

Liao, XB ^{[1
]}

机构：

[1] Univ Illinois, Coll Med, Dept Biochem & Mol Biol, Chicago, IL 60612 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1999年 / 289卷 / 04期

关键词：

NMR; structure; dynamics; Genesis; winged helix protein;

D O I：

10.1006/jmbi.1999.2819

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Genesis is an HNF-3/fkh homologous protein. By using multi-dimensional NMR techniques, we have obtained the solution structure and backbone dynamics of Genesis complexed with a 17 base-pair DNA. Our results indicate that both the local folding and dynamic properties of Genesis are perturbed when it binds to the DNA site. Our data show that a conserved flexible amino acid sequence (wing 1) makes dynamic contacts to DNA in the complex and a short helix is induced by Genesis-DNA interactions. Our data indicate that, unlike the HNF-3 gamma/DNA complex, a magnesium ion is not required in forming the stable Genesis-DNA complex. (C) 1999 Academic Press.

引用

页码：683 / 690

页数：8

共 25 条

[11] MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R
Billeter, M
Wuthrich, K
[J]. JOURNAL OF MOLECULAR GRAPHICS, 1996, 14 (01): : 51 - &
[12] HNF-3A, A HEPATOCYTE-ENRICHED TRANSCRIPTION FACTOR OF NOVEL STRUCTURE IS REGULATED TRANSCRIPTIONALLY
LAI, E
PREZIOSO, VR
SMITH, E
LITVIN, O
COSTA, RH
DARNELL, JE
[J]. GENES & DEVELOPMENT, 1990, 4 (08) : 1427 - 1436
[13] PROCHECK - A PROGRAM TO CHECK THE STEREOCHEMICAL QUALITY OF PROTEIN STRUCTURES
LASKOWSKI, RA
MACARTHUR, MW
MOSS, DS
THORNTON, JM
[J]. JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1993, 26 : 283 - 291
[14] LEUPIN W, 1990, FEBS LETT, V24, P313
[15] Evidence that the DNA binding specificity of winged helix proteins is mediated by a structural change in the amino acid sequence adjacent to the principal DNA binding helix
Marsden, I
Chen, Y
Jin, CW
Liao, XB
[J]. BIOCHEMISTRY, 1997, 36 (43) : 13248 - 13255
[16] Structural changes in the region directly adjacent to the DNA-binding helix highlight a possible mechanism to explain the observed changes in the sequence-specific binding of winged helix proteins
Marsden, I
Jin, CW
Liao, XB
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1998, 278 (02) : 293 - 299
[17] THE DNA-BINDING SPECIFICITY OF THE HEPATOCYTE NUCLEAR FACTOR 3/FORKHEAD DOMAIN IS INFLUENCED BY AMINO-ACID-RESIDUES ADJACENT TO THE RECOGNITION HELIX
OVERDIER, DG
PORCELLA, A
COSTA, RH
[J]. MOLECULAR AND CELLULAR BIOLOGY, 1994, 14 (04) : 2755 - 2766
[18] CHARACTERIZATION OF AMINO-ACID SIDE-CHAIN DYNAMICS IN A ZINC-FINGER PEPTIDE USING C-13 NMR-SPECTROSCOPY AND TIME-RESOLVED FLUORESCENCE SPECTROSCOPY
PALMER, AG
HOCHSTRASSER, RA
MILLAR, DP
RANCE, M
WRIGHT, PE
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (14) : 6333 - 6345
[19] Selective methyl group protonation of perdeuterated proteins
Rosen, MK
Gardner, KH
Willis, RC
Parris, WE
Pawson, T
Kay, LE
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1996, 263 (05) : 627 - 636
[20] The dissociation rate of a winged helix protein-DNA complex is influenced by non-DNA contact residues
Shiyanova, T
Liao, XB
[J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 362 (02) : 356 - 362

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