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Science 12 March 1993:
Vol. 259. no. 5101, pp. 1622 - 1625
DOI: 10.1126/science.8456286
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Articles

Science, Vol 259, Issue 5101, 1622-1625
Copyright © 1993 by American Association for the Advancement of Science

articles

Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation

JM Pongubala, C Van Beveren, S Nagulapalli, MJ Klemsz, McKercher SR, RA Maki, and ML Atchison

Department of Animal Biology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia 19104.

PU.1 recruits the binding of a second B cell-restricted nuclear factor, NF-EM5, to a DNA site in the immunoglobulin kappa 3' enhancer. DNA binding by NF-EM5 requires a protein-protein interaction with PU.1 and specific DNA contacts. Dephosphorylated PU.1 bound to DNA but did not interact with NF-EM5. Analysis of serine-to-alanine mutations in PU.1 indicated that serine 148 (Ser148) is required for protein-protein interaction. PU.1 produced in bacteria did not interact with NF-EM5. Phosphorylation of bacterially produced PU.1 by purified casein kinase II modified it to a form that interacted with NF-EM5 and that recruited NF-EM5 to bind to DNA. Phosphopeptide analysis of bacterially produced PU.1 suggested that Ser148 is phosphorylated by casein kinase II. This site is also phosphorylated in vivo. Expression of wild-type PU.1 increased expression of a reporter construct containing the PU.1 and NF-EM5 binding sites nearly sixfold, whereas the Ser148 mutant form only weakly activated transcription. These results demonstrate that phosphorylation of PU.1 at Ser148 is necessary for interaction with NF-EM5 and suggest that this phosphorylation can regulate transcriptional activity.


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K. S. Stranick, D. N. Zambas, A. S. Uss, R. W. Egan, M. M. Billah, and S. P. Umland (1997)
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I. Nuchprayoon, C. P. Simkevich, M. Luo, A. D. Friedman, and A. G. Rosmarin (1997)
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Differential Regulation of c-Myb-induced Transcription Activation by a Phosphorylation Site in the Negative Regulatory Domain.
M. R. Miglarese, A. F. Richardson, N. Aziz, and T. P. Bender (1996)
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Assembly and function of a TCR alpha enhancer complex is dependent on LEF-1-induced DNA bending and multiple protein-protein interactions..
K Giese, C Kingsley, J R Kirshner, and R Grosschedl (1995)
Genes & Dev. 9, 995-1008
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Involvement of the Ets Family Factor PU.1 in the Activation of Immunoglobulin Promoters.
H. Schwarzenbach, J. W. Newell, and P. Matthias (1995)
J. Biol. Chem. 270, 898-907
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The Drosophila E74 gene is required for the proper stage- and tissue-specific transcription of ecdysone-regulated genes at the onset of metamorphosis.
J. Fletcher and C. Thummel (1995)
Development 121, 1411-1421
   Abstract »    PDF »
Ets-related protein PU.1 regulates expression of the immunoglobulin J-chain gene through a novel Ets-binding element..
M K Shin and M E Koshland (1993)
Genes & Dev. 7, 2006-2015
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Tumor Necrosis Factor alpha -induced Phosphorylation of RelA/p65 on Ser529 Is Controlled by Casein Kinase II.
D. Wang, S. D. Westerheide, J. L. Hanson, and A. S. Baldwin Jr. (2000)
J. Biol. Chem. 275, 32592-32597
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Protein Phosphatase 2A Activates the HIV-2 Promoter through Enhancer Elements That Include the pets Site.
N. E. Faulkner, J. M. Hilfinger, and D. M. Markovitz (2001)
J. Biol. Chem. 276, 25804-25812
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AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain.
P. Rieske and J. M. R. Pongubala (2001)
J. Biol. Chem. 276, 8460-8468
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PU.1-mediated Transcription Is Enhanced by HMG-I(Y)-dependent Structural Mechanisms.
R. T. Lewis, A. Andreucci, and B. S. Nikolajczyk (2001)
J. Biol. Chem. 276, 9550-9557
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Cyclin A-dependent Phosphorylation of the ETS-related Protein, MEF, Restricts Its Activity to the G1 Phase of the Cell Cycle.
Y. Miyazaki, P. Boccuni, S. Mao, J. Zhang, H. Erdjument-Bromage, P. Tempst, H. Kiyokawa, and S. D. Nimer (2001)
J. Biol. Chem. 276, 40528-40536
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SHP1 Protein-tyrosine Phosphatase Inhibits gp91PHOX and p67PHOX Expression by Inhibiting Interaction of PU.1, IRF1, Interferon Consensus Sequence-binding Protein, and CREB-binding Protein with Homologous Cis Elements in the CYBB and NCF2 Genes.
B. Kautz, R. Kakar, E. David, and E. A. Eklund (2001)
J. Biol. Chem. 276, 37868-37878
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Evolution of hematopoiesis: Three members of the PU.1 transcription factor family in a cartilaginous fish, Raja eglanteria.
M. K. Anderson, X. Sun, A. L. Miracle, G. W. Litman, and E. V. Rothenberg (2001)
PNAS 98, 553-558
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Do lampreys have lymphocytes? The Spi evidence.
S. Shintani, J. Terzic, A. Sato, M. Saraga-Babic, C. O'hUigin, H. Tichy, and J. Klein (2000)
PNAS 97, 7417-7422
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