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
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.
DOI of Published Version
J Biol Chem. 1999 Nov 19;274(47):33580-6.
The Journal of biological chemistry
Tang L, Guo B, Javed A, Choi J, Hiebert SW, Lian JB, Van Wijnen AJ, Stein JL, Stein GS, Zhou GW. (1999). 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. GSBS Student Publications. https://doi.org/10.1074/jbc.274.47.33580. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/1228