ASSIGNMENT OF POSTTRANSLATIONAL MODIFICATIONS IN STREPTOLYSIN-S ANALOGUE

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 链球菌溶血素S（Streptolysin S，SLS）是由化脓性链球菌（Streptococcus Pyogenes）产生的一种强效溶细胞素。 SLS在毒力中起关键作用，并负责这些细菌的b-溶血性表型。 迄今为止，SLS的结构尚未确定。 以往的研究表明，SLS是一种高度后修饰的核糖体编码肽。 为了使肽变得溶细胞，将半胱氨酸、丝氨酸或苏氨酸中的一个或多个的侧链杂环化为五元噻唑或恶唑环。 通过质谱鉴定和绘制这些翻译后修饰的反复尝试都失败了。 本研究将使用NMR对重组产生的SLS类似物进行三重共振的顺序分配。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Streptolysin S (SLS) is a potent cytolysin produced by Streptococcus Pyogenes. SLS plays a key role in virulence and is responsible for the b-hemolytic phenotype of these bacteria. To date, the structure of SLS has not been identified. Previous studies have shown that SLS is a heavily posttranslationally modified ribosomally encoded peptide. In order for the peptide to become cytolytic the side chains of one or more of the cysteine, serine or threonines are heterocyclized into five membered thiazole or oxazole rings. Repeated attempts to identify and map these posttranslational modifications by mass spectrometry have failed. This study will use NMR to do a sequential assignment by triple resonance on a recombinantly produced SLS analogue.