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Blood, 15 January 2005, Vol. 105, No. 2, pp. 759-766. Prepublished online as a Blood First Edition Paper on July 15, 2004; DOI 10.1182/blood-2004-01-0001. This Article Full Text (PDF) Supplemental Videos All Versions of this Article: 2004-01-0001v1 105/2/759    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mi, J. Articles by Kupfer, G. M Search for Related Content PubMed PubMed Citation Articles by Mi, J. Articles by Kupfer, G. M Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted January 6, 2004 Accepted July 1, 2004 The Fanconi Anemia Core Complex Associates with Chromatin During S Phase Jun Mi and Gary M Kupfer* Department of Microbiology, University of Virginia Health System, Charlottesville, VA, USA Department of Microbiology, University of Virginia Health System, Charlottesville, VA, USA; Department of Pediatrics, University of Virginia Health System, Charlottesville, VA, USA * Corresponding author; email: gk9e{at}virginia.edu. Fanconi anemia (FA) is an autosomal recessive disease marked by bone marrow failure, birth defects, and cancer. The FA proteins FANCA, FANCC, FANCE, FANCF, FANCG, and FANCL proteins participate in a core complex. We have previously shown that several members of this complex bind to chromatin until mitosis, and this binding increases after DNA damage. The purpose of the present study was to determine the dynamics of complex movement between cytoplasm and nuclear compartments. Fluorescent-tagged versions of FANCA, FANCC, and FANCG colocalize in cytoplasm and nucleus, chiefly in chromatin. At the G1-S border, the FA core complex exists as foci on chromatin, progressively diffusing and migrating to the nuclear periphery and becoming completely excluded from condensed chromosomes by mitosis. Chromatin fiber analysis shows FA proteins diffusely staining along chromatin fibers during G1-S and S phase. Treatment with the DNA crosslinker mitomycin C results in a diffusion of foci and increased binding of complex proteins to chromatin, as well as diffuse and increased complex binding to chromatin fibers. These data are consistent with the idea that the FA proteins function at the level of chromatin during S phase to regulate and maintain genomic stability. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: N. G. Howlett, J. A. Harney, M. A. Rego, F. W. Kolling IV, and T. W. Glover Functional Interaction between the Fanconi Anemia D2 Protein and Proliferating Cell Nuclear Antigen (PCNA) via a Conserved Putative PCNA Interaction Motif J. Biol. Chem., October 16, 2009; 284(42): 28935 - 28942. [Abstract] [Full Text] [PDF] F. Yuan, J. El Hokayem, W. Zhou, and Y. Zhang FANCI Protein Binds to DNA and Interacts with FANCD2 to Recognize Branched Structures J. Biol. Chem., September 4, 2009; 284(36): 24443 - 24452. [Abstract] [Full Text] [PDF] N. B. Collins, J. B. Wilson, T. Bush, A. Thomashevski, K. J. Roberts, N. J. Jones, and G. M. Kupfer ATR-dependent phosphorylation of FANCA on serine 1449 after DNA damage is important for FA pathway function Blood, March 5, 2009; 113(10): 2181 - 2190. [Abstract] [Full Text] [PDF] J. Hejna, M. Holtorf, J. Hines, L. Mathewson, A. Hemphill, M. Al-Dhalimy, S. B. Olson, and R. E. 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