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
Graduate School of Biomedical Sciences; Program in Molecular Medicine; Department of Cell Biology
Medical Subject Headings
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
Life Sciences | Medicine and Health Sciences
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.
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Citation: J Biol Chem. 1999 Nov 19;274(47):33580-6.
Tang, Lei; Guo, Bo; Javed, Amjad; Choi, Je-Yong; Hiebert, Scott W.; Lian, Jane B.; Van Wijnen, Andre J.; Stein, Janet L.; Stein, Gary S.; and Zhou, G. Wayne, "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" (1999). GSBS Student Publications. 1228.