QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bléoo, S. Articles by Godbout, R. Search for Related Content PubMed PubMed Citation Articles by Bléoo, S. Articles by Godbout, R.

Vol. 12, Issue 10, 3046-3059, October 2001

Association of Human DEAD Box Protein DDX1 with a Cleavage Stimulation Factor Involved in 3'-End Processing of Pre-mRNA

Stacey Bléoo, Xuejun Sun, Michael J. Hendzel, John M. Rowe, Mary Packer, and Roseline Godbout^*

Department of Oncology, University of Alberta, Cross Cancer Institute, Edmonton, Alberta T6G 1Z2 Canada

DEAD box proteins are putative RNA helicases that function in all aspects of RNA metabolism, including translation, ribosome biogenesis, and pre-mRNA splicing. Because many processes involving RNA metabolism are spatially organized within the cell, we examined the subcellular distribution of a human DEAD box protein, DDX1, to identify possible biological functions. Immunofluorescence labeling of DDX1 demonstrated that in addition to widespread punctate nucleoplasmic labeling, DDX1 is found in discrete nuclear foci ~0.5 µm in diameter. Costaining with anti-Sm and anti-promyelocytic leukemia (PML) antibodies indicates that DDX1 foci are frequently located next to Cajal (coiled) bodies and less frequently, to PML bodies. Most importantly, costaining with anti-CstF-64 antibody indicates that DDX1 foci colocalize with cleavage bodies. By microscopic fluorescence resonance energy transfer, we show that labeled DDX1 resides within a Förster distance of 10 nm of labeled CstF-64 protein in both the nucleoplasm and within cleavage bodies. Coimmunoprecipitation analysis indicates that a proportion of CstF-64 protein resides in the same complex as DDX1. These studies are the first to identify a DEAD box protein associating with factors involved in 3'-end cleavage and polyadenylation of pre-mRNAs.

---

Online version of this article contains video material for Figures 2 and 5. Online version is available at www.molbiolcell.org.

^* Corresponding author. E-mail address: rgodbout{at}ualberta.ca.

---

Molecular Biology of the Cell
Vol. 12, 3046-3059, October 2001
Copyright © 2001 by The American Society for Cell Biology

This article has been cited by other articles:

				C. Rouget, C. Papin, and E. Mandart Cytoplasmic CstF-77 Protein Belongs to a Masking Complex with Cytoplasmic Polyadenylation Element-binding Protein in Xenopus Oocytes J. Biol. Chem., September 29, 2006; 281(39): 28687 - 28698. [Abstract] [Full Text] [PDF]

				L. Li, K. Roy, S. Katyal, X. Sun, S. Bleoo, and R. Godbout Dynamic Nature of Cleavage Bodies and Their Spatial Relationship to DDX1 Bodies, Cajal Bodies, and Gems Mol. Biol. Cell, March 1, 2006; 17(3): 1126 - 1140. [Abstract] [Full Text] [PDF]

				D. McDonald, G. Carrero, C. Andrin, G. de Vries, and M. J. Hendzel Nucleoplasmic {beta}-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J. Cell Biol., February 13, 2006; 172(4): 541 - 552. [Abstract] [Full Text] [PDF]

				G. Pinon-Lataillade, C. Masson, J. Bernardino-Sgherri, V. Henriot, P. Mauffrey, Y. Frobert, S. Araneda, and J. F. Angulo KIN17 encodes an RNA-binding protein and is expressed during mouse spermatogenesis J. Cell Sci., July 15, 2004; 117(16): 3691 - 3702. [Abstract] [Full Text] [PDF]

				M. I. Zarudnaya, I. M. Kolomiets, A. L. Potyahaylo, and D. M. Hovorun Downstream elements of mammalian pre-mRNA polyadenylation signals: primary, secondary and higher-order structures Nucleic Acids Res., March 1, 2003; 31(5): 1375 - 1386. [Abstract] [Full Text] [PDF]

				H.-C. Chen, W.-C. Lin, Y.-G. Tsay, S.-C. Lee, and C.-J. Chang An RNA Helicase, DDX1, Interacting with Poly(A) RNA and Heterogeneous Nuclear Ribonucleoprotein K J. Biol. Chem., October 18, 2002; 277(43): 40403 - 40409. [Abstract] [Full Text] [PDF]