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The LIM-only Protein Lmo2 is a Bridging Molecule Assembling an Erythroid, DNA-binding Complex Which Includes the TAL1, E47, GATA-1 and Ldb1/NLI Proteins

Overview
Journal EMBO J
Date 1997 Jun 2
PMID 9214632
Citations 354
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Abstract

The LIM-only protein Lmo2, activated by chromosomal translocations in T-cell leukaemias, is normally expressed in haematopoiesis. It interacts with TAL1 and GATA-1 proteins, but the function of the interaction is unexplained. We now show that in erythroid cells Lmo2 forms a novel DNA-binding complex, with GATA-1, TAL1 and E2A, and the recently identified LIM-binding protein Ldb1/NLI. This oligomeric complex binds to a unique, bipartite DNA motif comprising an E-box, CAGGTG, followed approximately 9 bp downstream by a GATA site. In vivo assembly of the DNA-binding complex requires interaction of all five proteins and establishes a transcriptional transactivating complex. These data demonstrate one function for the LIM-binding protein Ldb1 and establish a function for the LIM-only protein Lmo2 as an obligatory component of an oligomeric, DNA-binding complex which may play a role in haematopoiesis.

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References
1.
Wright W, Binder M, Funk W . Cyclic amplification and selection of targets (CASTing) for the myogenin consensus binding site. Mol Cell Biol. 1991; 11(8):4104-10. PMC: 361222. DOI: 10.1128/mcb.11.8.4104-4110.1991. View

2.
Hsu H, Cheng J, Chen Q, Baer R . Enhancer-binding activity of the tal-1 oncoprotein in association with the E47/E12 helix-loop-helix proteins. Mol Cell Biol. 1991; 11(6):3037-42. PMC: 360139. DOI: 10.1128/mcb.11.6.3037-3042.1991. View

3.
Funk W, Wright W . Cyclic amplification and selection of targets for multicomponent complexes: myogenin interacts with factors recognizing binding sites for basic helix-loop-helix, nuclear factor 1, myocyte-specific enhancer-binding factor 2, and COMP1 factor. Proc Natl Acad Sci U S A. 1992; 89(20):9484-8. PMC: 50156. DOI: 10.1073/pnas.89.20.9484. View

4.
Cheng J, Hsu H, Hwang L, Baer R . Products of the TAL1 oncogene: basic helix-loop-helix proteins phosphorylated at serine residues. Oncogene. 1993; 8(3):677-83. View

5.
Wright W, Funk W . CASTing for multicomponent DNA-binding complexes. Trends Biochem Sci. 1993; 18(3):77-80. DOI: 10.1016/0968-0004(93)90156-h. View