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蛋白质与来自大肠杆菌的完整核糖体亚基内的RNA的化学交联

Chemical cross-linking of protein to RNA within intact ribosomal subunits from Escherichia coli.

作者信息

Ulmer E, Meinke M, Ross A, Fink G, Brimacombe R

出版信息

Mol Gen Genet. 1978 Apr 6;160(2):183-93. doi: 10.1007/BF00267480.

DOI:10.1007/BF00267480
PMID:349353
Abstract

Bifunctional reagents, namely bis-(2-chloroethyl)-amine ("nitrogen mustard") and activated esters of 3-(2-bromo-3-oxobutane-1-sulphonyl)-propionic acid ("bromo-ketone reagent") are used to cross-linked protein to RNA within intact ribosomal subunits. The cross-linked proteins are analysed on two different two-dimensional gel electrophoresis sytems, and the existence of a stable cross-linkage is demonstrated by isolating cross-linked protein-oligonucleotide complexes from subunits containing 32P-labelled RNA. Proteins S3, S4, S5, S9/S11 and S13 from the 30S subunit, and proteins L1 and L2 from the 50S subunit were cross-linked to RNA by the nitrogen mustard, together with a number of other so far unresolved proteins. Correspondingly S3, S4, S7, S9/S11 and L12 were cross-linked by the bromoketone reagent, although in lower yield. The reagents should prove useful topographical studies on ribosomal subunits, and arguments are presented favouring the use of non-cleavable and relatively non-specific RNA-protein cross-linking reagents for such studies.

摘要

双功能试剂，即双（2-氯乙基）胺（“氮芥”）和3-（2-溴-3-氧代丁烷-1-磺酰基）-丙酸的活化酯（“溴酮试剂”），用于在完整的核糖体亚基内使蛋白质与RNA交联。交联后的蛋白质在两种不同的二维凝胶电泳系统上进行分析，并且通过从含有32P标记RNA的亚基中分离交联的蛋白质-寡核苷酸复合物来证明稳定交联的存在。30S亚基中的蛋白质S3、S4、S5、S9/S11和S13，以及50S亚基中的蛋白质L1和L2通过氮芥与RNA交联，还有许多其他尚未解析的蛋白质。相应地，S3、S4、S7、S9/S11和L12通过溴酮试剂交联，尽管产率较低。这些试剂应被证明对核糖体亚基的拓扑学研究有用，并且提出了支持使用不可裂解且相对非特异性的RNA-蛋白质交联试剂进行此类研究的论据。

相似文献

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Chemical cross-linking of protein to RNA within intact ribosomal subunits from Escherichia coli.蛋白质与来自大肠杆菌的完整核糖体亚基内的RNA的化学交联
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Crosslinking of ribosomal proteins S4, S5, S7, S8, S11, S12 and S18 to domains 1 and 2 of 16S rRNA in the Escherichia coli 30S particle.核糖体蛋白S4、S5、S7、S8、S11、S12和S18与大肠杆菌30S颗粒中16S rRNA的结构域1和结构域2的交联。
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