Crystal structure of the nuclear matrix targeting signal of the transcription factor acute myelogenous leukemia-1/polyoma enhancer-binding protein 2alphaB/core binding factor alpha2.

Tang L, Guo B, Javed A, Choi JY, Hiebert S, Lian JB, van Wijnen AJ, Stein JL, Stein GS, Zhou GW
J Biol Chem. 1999 274 (47): 33580-6

PMID: 10559245 · DOI:10.1074/jbc.274.47.33580

Transcription factors of the acute myelogenous leukemia (AML)/polyoma enhancer-binding protein (PEBP2alpha)/core-binding factor alpha (CBFA) class are key transactivators of tissue-specific genes of the hematopoietic and bone lineages. AML-1/PEBP2alphaB/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.

MeSH Terms (14)

Amino Acid Sequence Antigens, Nuclear Core Binding Factor Alpha 2 Subunit DNA-Binding Proteins Glutathione Transferase Glycine Molecular Sequence Data Neoplasm Proteins Nuclear Proteins Protein Conformation Proto-Oncogene Proteins Recombinant Fusion Proteins Sequence Homology, Amino Acid Transcription Factors

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