Terminal, and telomere-associated proteins of pAL1, a linear plasmid from Arthrobacter nitroguajacolicus Rü61a

pAL1 的末端和端粒相关蛋白，pAL1 是来自硝化鳄梨节杆菌 Rü61a 的线性质粒

• 批准号: 5449768
• 负责人: Professor Dr. Friedhelm Meinhardt
• 金额: --
• 依托单位: Institut für Molekulare Mikrobiologie und Biotechnologie
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2005
• 资助国家: 德国
• 起止时间: 2004-12-31 至 2008-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/5449768?language=en
• 关键词: Terminal; telomere; associated; proteins; pAL1

Based on sequence analysis of the novel linear plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a, we propose that a subgroup of actinomycetal linear plasmids, represented by pBD2[1] and pAL1, have evolved a unique mechanism of telomere patching, involving an unprecedented telomere associated protein (Tap). The proteins of this telomere patching system may share some common motifs with the Tap and Tpg (terminal telomere binding) proteins of Streptomyces linear replicons, but appear to be significantly different, e.g., in their domain structure. The putative TappAL1 contains large additional domain(s) and may be distantly related to B-type DNA polymerases. The goal of this first project on an Arthrobacter linear plasmid is to identify all proteins bound to the termini and involved in telomere patching, and to characterize their function. We are especially interested in investigating the role of the presumptive TappAL1 in interacting with the DNA and/or the terminal protein(s) (TpgpAL1), and its potential catalytic activity in telomere patching. The main objectives are: Identification of the Tpg protein(s); identification of (further) proteins with specific affinity to the telomeres; expression cloning of tpgpAL1 and tappAL1; functional studies (i) addressing the specificity of DNA binding of TpgpAL1, TappAL1 (and/or other proteins), (ii) assessing the interaction of TpgpAL1 and TappAL1, and (iii) analysing whether TappAL1 shows desoxynucleotidylation (primase, polymerase) activity. The ultimate goal is to understand the mechanism of telomere patching. [1] Stecker C, Johann A, Herzberg C, Averhoff B, Gottschalk G (2003) J Bacteriol 185: 5269-5274.

基于对节杆菌Nitroguajacolicus Rü 61 a的新型线性质粒pAL 1的序列分析，我们提出以pBD 2 [1]和pAL 1为代表的放线菌线性质粒亚组已经进化出独特的端粒修补机制，涉及前所未有的端粒相关蛋白（Tap）。这种端粒修补系统的蛋白质可能与链霉菌线性复制子的Tap和Tpg（末端端粒结合）蛋白质共享一些共同的基序，但似乎是显著不同的，例如，在它们的域结构中。TappAL 1含有较大的额外结构域，可能与B型DNA聚合酶有较远的亲缘关系。这个关于节杆菌线性质粒的第一个项目的目标是鉴定所有与末端结合并参与端粒修补的蛋白质，并表征其功能。我们特别感兴趣的是研究推定的TappAL 1在与DNA和/或末端蛋白（TpgpAL 1）相互作用中的作用，以及其在端粒修补中的潜在催化活性。主要目标是：鉴定Tpg蛋白;鉴定对端粒具有特异性亲和力的（其他）蛋白; tpgpAL 1和TappAL 1的表达克隆;功能研究（i）解决TpgpAL 1、TappAL 1（和/或其他蛋白）的DNA结合特异性，（ii）评估TpgpAL 1和TappAL 1的相互作用，和（iii）分析TappAL 1是否显示脱氧核苷酸化（引发酶、聚合酶）活性。最终目标是了解端粒修补的机制。[1]Stecker C，Johann A，Herzberg C，Averhoff B，Gottschalk G（2003）J Bacteriol 185：5269-5274.