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Prepublished online as a Blood First Edition Paper on March 20, 2003; DOI 10.1182/blood-2002-11-3517. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-11-3517v1 102/1/136    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Gordon, S. M. Articles by Buchwald, M. Search for Related Content PubMed PubMed Citation Articles by Gordon, S. M. Articles by Buchwald, M. Related Collections Hematopoiesis and Stem Cells Neoplasia Red Cells Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 July 2003, Vol. 102, No. 1, pp. 136-141 HEMATOPOIESIS Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems Susan M. Gordon, and Manuel Buchwald From the Program in Genetics and Genomic Biology, Research Institute, Hospital for Sick Children, Toronto, ON, Canada; and the Department of Molecular and Medical Genetics, University of Toronto, ON, Canada. Fanconi anemia (FA) is an autosomal recessive syndrome characterized by progressive bone marrow failure and cancer predisposition. Eight FA complementation groups have been identified. The FANCA, FANCC, FANCE, FANCF, and FANCG proteins form a nuclear complex required for the monoubiquination of the FANCD2 protein. To investigate the architecture of the FA protein complex, the yeast 2-hybrid system was used to map contact points of the FANCA/FANCG, FANCC/FANCE, and FANCF/FANCG interactions. FANCG was shown to interact with both the amino-terminus of FANCA and the carboxyl-terminal region of FANCF. A FANCG mutant truncated at the carboxyl-terminus retained the ability to interact with FANCA. The interaction between FANCG and FANCF was ablated by a Leu71Pro mutant of FANCG. A central region of FANCE was sufficient for FANCC binding. A Leu554Pro mutant of FANCC failed to interact with FANCE. To further examine complex assembly, the yeast 3-hybrid system was used to investigate the ability of FANCG to act as a molecular bridge in mediating interaction between other FA proteins. FANCG was able to mediate interaction between FANCA and FANCF, as well as between monomers of FANCA. Direct interaction between FANCE and FANCD2 was also demonstrated in the yeast 2-hybrid system. This interaction involving an amino-terminal region of FANCD2 may provide a link between the FA protein complex and its downstream targets. (Blood. 2003;102:136-141) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: New insights from Fanconi anemia Alan D'Andrea Blood 2003 102: 1. [Full Text] [PDF] This article has been cited by other articles: C. S. Tremblay, F. F. Huang, O. Habi, C. C. Huard, C. Godin, G. Levesque, and M. Carreau HES1 is a novel interactor of the Fanconi anemia core complex Blood, September 1, 2008; 112(5): 2062 - 2070. [Abstract] [Full Text] [PDF] R. K. Nookala, S. Hussain, and L. Pellegrini Insights into Fanconi Anaemia from the structure of human FANCE Nucleic Acids Res., March 12, 2007; 35(5): 1638 - 1648. [Abstract] [Full Text] [PDF] S. Seki, M. Ohzeki, A. Uchida, S. Hirano, N. Matsushita, H. Kitao, T. Oda, T. Yamashita, N. Kashihara, A. Tsubahara, et al. 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