Crystal structure of the nuclear matrix targeting signal of the transcription factor acute myelogenous leukemia-1/polyoma enhancer-binding protein 2αB/core binding factor α2

Lei Tang, Bo Guo, Amjad Javed, Je Yong Choi, Scott Hiebert, Jane B. Lian, André J. Van Wijnen, Janet L. Stein, Gary S. Stein, G. Wayne Zhou

Research output: Contribution to journalArticle

66 Scopus citations

Abstract

Transcription factors of the acute myelogenous leukemia (AML)/polyoma enhancer-binding protein (PEBP2α)/core-binding factor α (CBFA) class are key transactivators of tissue-specific genes of the hematopoietic and bone lineages. AML-1/PEBP2αB/CBFA2 proteins participating in transcription are associated with the nuclear matrix. This association is solely dependent on a highly conserved C-terminal protein segment, designated the nuclear matrix targeting signal (NMTS). The NMTS of AML-1 is physically distinct from the nuclear localization signal, operates autonomously, and supports transactivation. Our data indicate that the related AML-3 and AML-2 proteins are also targeted to the nuclear matrix in situ by analogous C-terminal domains. Here we report the first crystal structure of an NMTS in an AML-1 segment fused to glutathione S-transferase. The model of the NMTS consists of two loops connected by a flexible U-shaped peptide chain.

Original languageEnglish (US)
Pages (from-to)33580-33586
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number47
DOIs
StatePublished - Nov 19 1999

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Tang, L., Guo, B., Javed, A., Choi, J. Y., Hiebert, S., Lian, J. B., Van Wijnen, A. J., Stein, J. L., Stein, G. S., & Zhou, G. W. (1999). Crystal structure of the nuclear matrix targeting signal of the transcription factor acute myelogenous leukemia-1/polyoma enhancer-binding protein 2αB/core binding factor α2. Journal of Biological Chemistry, 274(47), 33580-33586. https://doi.org/10.1074/jbc.274.47.33580