AFM study of Escherichia coli RNA polymerase σ70 subunit aggregation

被引:3
作者
Dubrovin, Evgeniy V. [1 ]
Koroleva, Olga N. [2 ]
Khodak, Yulia A. [3 ]
Kuzmina, Natalia V. [1 ]
Yaminsky, Igor V. [1 ]
Drutsa, Valeriy L. [3 ]
机构
[1] Moscow MV Lomonosov State Univ, Dept Phys Polymers & Crystals, Fac Phys, Moscow 119991, Russia
[2] Moscow MV Lomonosov State Univ, Fac Chem, Moscow 119991, Russia
[3] Moscow MV Lomonosov State Univ, Belozersky Inst Physicochem Biol, Moscow 119991, Russia
关键词
E. coli RNA polymerase sigma(70) subunit; Self-assembly; Atomic force microscopy; Amyloid fibrils; Congo red; AMYLOID FIBRILS; PROTEIN AGGREGATION; CORE ENZYME; TRANSCRIPTION; ORGANIZATION; OLIGOMERS; FRAGMENT; DISEASES;
D O I
10.1016/j.nano.2011.05.014
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
The self-assembly of Escherichia coli RNA polymerase sigma(70) subunit was investigated using several experimental approaches. A novel rodlike shape was reported for sigma(70) subunit aggregates. Atomic force microscopy reveals that these aggregates, or sigma(70) polymers, have a straight rodlike shape 5.4 nm in diameter and up to 300 nm in length. Atomic force microscopy data, Congo red binding assay, and sodium dodecyl sulfate gel electrophoresis confirm the amyloid nature of observed aggregates. The process of formation of rodlike structures proceeds spontaneously under nearly physiological conditions. E. coli RNA polymerase sigma(70) subunit may be an interesting object for investigation of amyloidosis as well as for biotechnological applications that exploit self-assembled bionanostructures. Polymerization of sigma(70) subunit may be a competitive process with its three-dimensional crystallization and association with core RNA polymerase. From the Clinical Editor: In this basic science study, the self-assembly of Escherichia coli RNA polymerase sigma(70) subunit was investigated using atomic force microscopy and other complementary approaches. (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码:54 / 62
页数:9
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