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Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Wertheim cung cấp cho các bạn kiến thức về ngành y đề tài: The microbial selenoproteome of the Sargasso Sea. | Research The microbial selenoproteome of the Sargasso Sea Yan Zhang Dmitri E Fomenko and Vadim N Gladyshev Open Access Address Department of Biochemistry University of Nebraska Lincoln NE 68588-0664 USA. Correspondence Vadim N Gladyshev. E-mail vgladyshev1@unl.edu Published 29 March 2005 Genome Biology 2005 6 R37 doi l0.l 186 gb-2005-6-4-r37 The electronic version of this article is the complete one and can be found online at http genomebiology.com 2005 6 4 R37 Received 11 January 2005 Revised 7 February 2005 Accepted 21 February 2005 2005 Zhang et al. licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Selenocysteine Sec is a rare amino acid which occurs in proteins in major domains of life. It is encoded by TGA which also serves as the signal for termination of translation precluding identification of selenoprotein genes by available annotation tools. Information on full sets of selenoproteins selenoproteomes is essential for understanding the biology of selenium. Herein we characterized the selenoproteome of the largest microbial sequence dataset the Sargasso Sea environmental genome project. Results We identified 310 selenoprotein genes that clustered into 25 families including 101 new selenoprotein genes that belonged to 15 families. Most of these proteins were predicted redox proteins containing catalytic selenocysteines. Several bacterial selenoproteins previously thought to be restricted to eukaryotes were detected by analyzing eukaryotic and bacterial SECIS elements suggesting that eukaryotic and bacterial selenoprotein sets partially overlapped. The Sargasso Sea microbial selenoproteome was rich in selenoproteins and its composition was different from that observed in the combined set of completely
