Mitf mi-enu122 is a missense mutation in the HLH dimerization domain

Mammalian Genome

Volumn 9, Issue 3, 1998, Pages 250-252

  Steingrímsson, Eiríkur ^a   Favor, Jack ^b   Ferré D’Amaré, Adrian F ^c   Copeland, Neal G ^a   Jenkins, Nancy A ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b INSTITUTE OF EPIDEMIOLOGY   (Germany)

^c YALE UNIVERSITY   (United States)

Author keywords

Coat Color; Coat Color Phenotype; Hydrophobic Core; Microphthalmia; Pigmentary Disturbance

Indexed keywords

DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; MICROPHTHALMIA ASSOCIATED TRANSCRIPTION FACTOR; MITF PROTEIN, MOUSE; TRANSCRIPTION FACTOR;

ANIMAL; ARTICLE; BINDING SITE; C3H MOUSE; CHEMICAL STRUCTURE; DIMERIZATION; FEMALE; GENETICS; MALE; MOUSE; MUTATION;

ANIMALS; BINDING SITES; DIMERIZATION; DNA-BINDING PROTEINS; FEMALE; HELIX-LOOP-HELIX MOTIFS; MALE; MICE; MICE, INBRED C3H; MICROPHTHALMIA-ASSOCIATED TRANSCRIPTION FACTOR; MODELS, MOLECULAR; MUTATION; TRANSCRIPTION FACTORS;

EID: 0032011327     PISSN: 09388990     EISSN: 14321777     Source Type: Journal    
DOI: 10.1007/s003359900736     Document Type: Article

References (14)

1. Ferré-D’Amaré AR, Prendergast GC, Ziff EB, Burley SK (1993) Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363, 38–45 DOI: 10.1038/363038a0
2. Ferré-D’Amaré AR, Pognonec P, Roeder RG, Burley SK (1994) Structure and function of the b/HLH/Z domain of USF. EMBO J 13, 180–189
3. Hemesath TJ, Steingrímsson E, McGill G, Hansen MJ, Vaught J, Hodgkinson CA, Arnheiter H, Copeland NG, Jenkins NA, Fisher DE (1994) crophthalmia, a critical factor in melanocyte development, defines a discrete transcription factor family. Genes Dev 8, 2770–2780 DOI: 10.1101/gad.8.22.2770
4. Hodgkinson CA, Moore KJ, Nakayama A, Steingrímsson E, Copeland NG, Jenkins NA, Arnheiter H (1993) Mutations at the mouse microphthalmia locus are associated with defects in a gene encoding a novel basic-helix-loop-helix-zipper protein. Cell 74, 395–404 DOI: 10.1016/0092-8674(93)90429-T
5. Hughes MJ, Lingrel JB, Krakowsky JM, Anderson KP (1993) A helix-loop-helix transcription factor-like gene is located at the mi locus. J Biol Chem 268, 20687–20690
6. Lim WA, Sauer RT (1991) The role of internal packing interactions in determining the structure and stability of a protein. J Mol Biol 219, 359–376 DOI: 10.1016/0022-2836(91)90570-V
7. Marker PC, Seung K, Bland AE, Russell LB, Kingsley DM (1997) Spectrum of Bmp5 mutations from germline mutagenesis experiments in mice. Genetics 145, 435–443
8. Moore KJ (1995) Insight into the microphthalmia gene. Trends Genet 11, 442–448 DOI: 10.1016/S0168-9525(00)89143-X
9. Shirakata M, Friedman FK, Wei Q, Paterson BM (1993) Dimerization specificity of myogenic helix-loop-helix DNA-binding factors directed by nonconserved hydrophilic residues. Genes Dev 7, 2456–2470 DOI: 10.1101/gad.7.12a.2456
10. Steingrímsson E, Moore KJ, Lamoreux ML, Ferré-D’Amaré AR, Burley SK, Zimring DC, Skow LC, Hodgkinson CA, Arnheiter H, Copeland NG, Jenkins NA (1994) Molecular basis of mouse microphthalmia (mi) mutations helps explain their developmental and phenotypic consequences. Nat Genet 8, 256–263 DOI: 10.1038/ng1194-256
11. b mutation identifies a role for the HLH domain in DNA binding in addition to its role in protein dimerization. EMBO J 15, 6280–6289
12. Takebayashi K, Chida K, Tsukamoto I, Morii E, Munakata H, Arnheiter H, Kuroki T, Kitamura Y, Nomura S (1996) The recessive phenotype displayed by a dominant negative microphthalmia-associated transcription factor mutant is a result of impaired nuclear localization potential. Mol Cell Biol 16, 1203–1211
13. Tassabehji M, Newton VE, Read AP (1994) Waardenburg syndrome type 2 caused by mutations in the human microphthalmia (MITF) gene. Nat Genet 8, 251–255 DOI: 10.1038/ng1194-251
14. Tassabehji M, Newton VE, Liu X-Z, Brady A, Donnai D, Krajewska-Walasek M, Murday V, Norman A, Obersztyn E, Reardon W, Rice JC, Trembath R, Wieacker P, Whiteford M, Winter R, Read AP (1995) The mutational spectrum in Waardenburg syndrome. Hum Mol Genet 4, 2131–2137 DOI: 10.1093/hmg/4.11.2131