Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Plant NBS-LRR proteins: adaptable guards. | Review Plant NBS-LRR proteins adaptable guards Leah McHale Xiaoping Tan Patrice Koehl and Richard W Michelmore Address The Genome Center University of California Davis CA 95616 USA. Correspondence Richard W Michelmore. Email rwmichelmore@ Published 26 April 2006 Genome Biology 2006 7 212 doi gb-2006-7-4-212 The electronic version of this article is the complete one and can be found online at http 2006 7 4 212 2006 BioMed Central Ltd Abstract The majority of disease resistance genes in plants encode nucleotide-binding site leucine-rich repeat NBS-LRR proteins. This large family is encoded by hundreds of diverse genes per genome and can be subdivided into the functionally distinct TIR-domain-containing TNL and CC-domain-containing CNL subfamilies. Their precise role in recognition is unknown however they are thought to monitor the status of plant proteins that are targeted by pathogen effectors. Most of the disease resistance genes R genes in plants cloned to date encode nucleotide-binding site leucine-rich repeat NBS-LRR proteins characterized by nucleotide-binding site NBS and leucine-rich repeat LRR domains as well as variable amino- and carboxy-terminal domains Figure 1 . These large abundant proteins are involved in the detection of diverse pathogens including bacteria viruses fungi nematodes insects and oomycetes. There have been numerous extensive reviews since the first NBS-LRR-encoding genes were cloned from plants in 1994 for example 1-5 . This article aims to provide a current overview of the structure and function of this protein family as well as to highlight recent advances. Plant NBS-LRR proteins are similar in sequence to members of the mammalian nucleotide-binding oligomerization domain NOD -LRR protein family also called CARD transcription enhancer R purine -binding pyrin lots of leucine repeats CATERPILLER proteins which function in inflammatory and immune responses 6 . But although mammalian NOD-LRR proteins .
