Literature DB >> 18323601

Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA.

Jose Henrique Pereira1, Sung Chul Ha, Sung-Hou Kim.   

Abstract

The Brn-5 protein plays an important role in the control of cellular development and belongs to a class of transcription factors that usually contain two domains: the POU homeodomain (POU(HD)) and the POU-specific domain (POU(S)). Since high-quality crystals suitable for crystallographic studies of the proteins of this class are difficult to obtain, all the known structural information available is for POU(HD) and/or POU(S). This paper describes several critical steps that allowed the production of high-quality crystals of the full-length Brn-5 protein complexed with its cognate DNA.

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Year:  2008        PMID: 18323601      PMCID: PMC2374152          DOI: 10.1107/S1744309108003370

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  15 in total

1.  Crystallization of the yeast MATalpha2/MCM1/DNA ternary complex: general methods and principles for protein/DNA cocrystallization.

Authors:  S Tan; Y Hunziker; L Pellegrini; T J Richmond
Journal:  J Mol Biol       Date:  2000-04-07       Impact factor: 5.469

2.  Crystallization of redox-insensitive Oct1 POU domain with different DNA-response elements.

Authors:  A Reményi; E Pohl; H R Schöler; M Wilmanns
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2001-10-25

Review 3.  Transcription factors: structural families and principles of DNA recognition.

Authors:  C O Pabo; R T Sauer
Journal:  Annu Rev Biochem       Date:  1992       Impact factor: 23.643

Review 4.  POU-domain transcription factors: pou-er-ful developmental regulators.

Authors:  M G Rosenfeld
Journal:  Genes Dev       Date:  1991-06       Impact factor: 11.361

Review 5.  DNA binding specificity of homeodomains.

Authors:  A Laughon
Journal:  Biochemistry       Date:  1991-12-03       Impact factor: 3.162

Review 6.  Regulation of transcription and cell identity by POU domain proteins.

Authors:  G Ruvkun; M Finney
Journal:  Cell       Date:  1991-02-08       Impact factor: 41.582

7.  Use of T7 RNA polymerase to direct expression of cloned genes.

Authors:  F W Studier; A H Rosenberg; J J Dunn; J W Dubendorff
Journal:  Methods Enzymol       Date:  1990       Impact factor: 1.600

8.  The POU domain is a bipartite DNA-binding structure.

Authors:  R A Sturm; W Herr
Journal:  Nature       Date:  1988-12-08       Impact factor: 49.962

9.  Involvement of mPOU (Brn-5), a class VI POU protein, in the gene expression of Pit-1 as well as PRL.

Authors:  Keizo Toda; Daisuke Yamamoto; Mariko Fumoto; Nobuko Ikeshita; Elizabeth Henny Herningtyas; Keiji Iida; Yutaka Takahashi; Hidesuke Kaji; Kazuo Chihara; Yasuhiko Okimura
Journal:  Mol Cell Endocrinol       Date:  2007-09-08       Impact factor: 4.102

10.  The DNA binding specificity of the bipartite POU domain and its subdomains.

Authors:  C P Verrijzer; M J Alkema; W W van Weperen; H C Van Leeuwen; M J Strating; P C van der Vliet
Journal:  EMBO J       Date:  1992-12       Impact factor: 11.598

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