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, Andre J van Wijnen, Janet L. Stein, Gary S. Stein, G. Wayne Zhou

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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
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

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