Identification of a conserved protein that interacts with specific LIM homeodomain transcription factors

Paul W. Howard, Richard Maurer

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

Lhx3, a member of the LIM homeodomain family of transcription factors, is required for development of the pituitary and is implicated in the transcription of pituitary-specific hormone genes. In this report we describe a novel gene product, SLB, that selectively interacts with Lhx3 and the closely related LIM factor, Lhx4. The SLB cDNA encodes a 1749-residue protein that contains seven WD40 repeats near the amino terminus and a putative nuclear localization signal and does not contain other recognizable motifs. SLB is expressed in a tissue-specific manner with the highest concentrations of SLB mRNA in the testis and pituitary cells. We demonstrate that SLB specifically binds to Lhx3 and Lhx4 with high affinity both in vitro and in vivo. SLB has much lower affinity or no detectable affinity for other LIM domains. An expression vector for a fragment of SLB containing the LIM- interaction domain was shown to reduce expression of Lhx3-responsive reporter genes. The ability of the LIM-interacting domain of SLB to alter reporter gene activity as well as the tissue-specific expression and the specificity of SLB binding to LIM factors suggest a possible role in modulating the transcriptional activity of specific LIM factors.

Original languageEnglish (US)
Pages (from-to)13336-13342
Number of pages7
JournalJournal of Biological Chemistry
Volume275
Issue number18
DOIs
StatePublished - May 5 2000

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Reporter Genes
Transcription Factors
Genes
Nuclear Localization Signals
Pituitary Hormones
Testis
Proteins
Complementary DNA
Tissue
Messenger RNA
Transcription
Hormones
WD40 Repeats
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of a conserved protein that interacts with specific LIM homeodomain transcription factors. / Howard, Paul W.; Maurer, Richard.

In: Journal of Biological Chemistry, Vol. 275, No. 18, 05.05.2000, p. 13336-13342.

Research output: Contribution to journalArticle

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