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Journal of Cell Science, Vol 113, Issue 24 4523-4531, Copyright © 2000 by Company of Biologists
JOURNAL ARTICLES |
XH Lei, X Shen, XQ Xu and HS Bernstein
Department of Pediatrics, Cardiovascular Research Institute and Cancer Center, University of California, San Francisco, Box 0130, San Francisco, California 94143-0130, USA.
G(2)/M progression requires coordinated expression of many gene products, but little is known about the transcriptional regulators involved. We recently identified human Cdc5, a positive regulator of G(2)/M in mammalian cells. We also demonstrated the presence of a latent activation domain in its carboxyl terminus, suggesting that human Cdc5 regulates G(2)/M through transcriptional activation. Despite the presence of a DNA binding domain, studies by others have failed to identify a preferential binding site for Cdc5 family members. In addition, Cdc5 recently has been associated with the splicesome in several organisms, suggesting that it may not act through DNA binding. We now report the identification of a 12 bp sequence to which human Cdc5 binds specifically and with high affinity through its amino terminus. We show that this DNA-protein interaction is capable of activating transcription. We also used a selection system in yeast to identify human genomic fragments that interact with human Cdc5. Several of these contained sequences similar to the binding site. We demonstrate that these bind human Cdc5 with similar specificity and affinity. These experiments provide the first evidence that Cdc5 family members can act as site-specific DNA binding proteins, and that human Cdc5 may interact with specific, low abundance sequences in the human genome. This raises the possibility that Cdc5 proteins may participate in more than one process necessary for regulated cell division.
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  M. Hlaing, P. Spitz, K. Padmanabhan, B. Cabezas, C. S. Barker, and H. S. Bernstein E2F-1 Regulates the Expression of a Subset of Target Genes during Skeletal Myoblast Hypertrophy J. Biol. Chem., October 15, 2004; 279(42): 43625 - 43633. [Abstract] [Full Text] [PDF]
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X. Sun, H. Zhang, D. Wang, D. Ma, Y. Shen, and Y. Shang DLP, a Novel Dim1 Family Protein Implicated in Pre-mRNA Splicing and Cell Cycle Progression J. Biol. Chem., July 30, 2004; 279(31): 32839 - 32847. [Abstract] [Full Text] [PDF]
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 P. Ajuh and A. I. Lamond Identification of peptide inhibitors of pre-mRNA splicing derived from the essential interaction domains of CDC5L and PLRG1 Nucleic Acids Res., November 1, 2003; 31(21): 6104 - 6116. [Abstract] [Full Text] [PDF]
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M. Hlaing, X. Shen, P. Dazin, and H. S. Bernstein The Hypertrophic Response in C2C12 Myoblasts Recruits the G1 Cell Cycle Machinery J. Biol. Chem., June 21, 2002; 277(26): 23794 - 23799. [Abstract] [Full Text] [PDF]
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H. Engemann, V. Heinzel, G. Page, U. Preuss, and K. H. Scheidtmann DAP-like kinase interacts with the rat homolog of Schizosaccharomyces pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for G2/M phase transition Nucleic Acids Res., March 15, 2002; 30(6): 1408 - 1417. [Abstract] [Full Text] [PDF]
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P. Ajuh, J. Sleeman, J. Chusainow, and A. I. Lamond A Direct Interaction between the Carboxyl-terminal Region of CDC5L and the WD40 Domain of PLRG1 Is Essential for Pre-mRNA Splicing J. Biol. Chem., November 2, 2001; 276(45): 42370 - 42381. [Abstract] [Full Text] [PDF]
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T. Berge, S. L. Bergholtz, K. B. Andersson, and O. S. Gabrielsen A novel yeast system for in vivo selection of recognition sequences: defining an optimal c-Myb-responsive element Nucleic Acids Res., October 15, 2001; 29(20): e99 - e99. [Abstract] [Full Text] [PDF]
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