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: 5449744
• 负责人: Professorin Dr. Susanne Fetzner
• 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 2009-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/5449744?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.

基于关节炎杆菌的新型线性质粒PAL1的序列分析，我们提出的是，由PBD2 [1]和PAL1代表的放线菌的线性质粒的亚组，已经进化出了远程保留贴剂的独特机制，涉及远程贴剂的蛋白蛋白蛋白蛋白质（涉及远距离的蛋白酶）。该端粒补丁系统的蛋白质可能与链霉菌线性复制品的TAP和TPG（末端端粒结合）蛋白共享一些常见基序，但似乎在其域结构中有显着差异。推定的Tappal1包含大型额外结构域，并且可能与B型DNA聚合酶遥远有关。第一个项目在关节杆菌线性质粒上的目标是识别与术语结合并参与端粒修补的所有蛋白质，并表征其功能。我们特别有兴趣研究假定Tappal1与DNA和/或末端蛋白（s）（TPGPAL1）相互作用的作用，以及其在端粒贴片中的潜在催化活性。主要目标是：TPG蛋白的识别；鉴定（进一步的）蛋白质对端粒具有特定亲和力； TPGPAL1和TAPAPPAL1的表达克隆；功能研究（i）解决TPGPAL1，TAPPAL1（和/或其他蛋白质）的DNA结合的特异性，（ii）评估TPGPAL1和TAPPAL1的相互作用，以及（iii）分析Tappal1是否显示脱氧核苷酸化（原始酶，聚合酶，聚合酶）的活性。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。