Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Novel G-protein-coupled receptor-like proteins in the plant pathogenic fungus Magnaporthe grisea. | Research Open Access Novel G-protein-coupled receptor-like proteins in the plant pathogenic fungus Magnaporthe grisea Resham D Kulkarni Michael R Thon Huaqin Pan and Ralph A Dean Addresses Fungal Genomics Laboratory Center for Integrated Fungal Research North Carolina State University Raleigh NC 27695 USA. Current address Bioinformatics Program Research Computing Division RTI International 3040 Cornwallis Road Research Triangle Park NC 27707 USA. Program for Biology of Filamentous Fungi Department of Plant Pathology and Microbiology Texas A M University College Station TX 77843 USA. Correspondence Ralph A Dean. E-mail radean2@ Published 2 March 2005 Genome Biology 2005 6 R24 The electronic version of this article is the complete one and can be found online at http 2005 6 3 R24 Received 15 November 2004 Revised 30 December 2004 Accepted 31 January 2005 2005 Kulkarni et al. licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The G-protein-coupled receptors GPCRs are one of the largest protein families in human and other animal genomes but no more than 10 GPCRs have been characterized in fungi. Do fungi contain only this handful or are there more receptors to be discovered We asked this question using the recently sequenced genome of the fungal plant pathogen Magnaporthe grisea. Results Proteins with significant similarity to fungus-specific and other eukaryotic GPCRs were identified in M. grisea. These included homologs of known fungal GPCRs the cAMP receptors from Dictyostelium and a steroid receptor mPR. We also identified a novel class of receptors typified by PTH1 1 a cell-surface integral membrane protein required for pathogenicity. PTH11 has seven transmembrane regions and
