无机多聚磷酸盐在大肠杆菌中由Lon蛋白酶促进核糖体蛋白降解过程中的作用。

Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli.

作者信息

Kuroda A, Nomura K, Ohtomo R, Kato J, Ikeda T, Takiguchi N, Ohtake H, Kornberg A

机构信息

Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-4-1 Kagamiyama, Hiroshima 739-8527, Japan.

出版信息

Science. 2001 Jul 27;293(5530):705-8. doi: 10.1126/science.1061315.

DOI:10.1126/science.1061315

PMID:11474114

Abstract

Inorganic polyphosphate (polyP), a polymer of hundreds of phosphate (Pi) residues, accumulates in Escherichia coli in response to stresses, including amino acid starvation. Here we show that the adenosine 5'-triphosphate-dependent protease Lon formed a complex with polyP and degraded most of the ribosomal proteins, including S2, L9, and L13. Purified S2 also bound to polyP and formed a complex with Lon in the presence of polyP. Thus, polyP may promote ribosomal protein degradation by the Lon protease, thereby supplying the amino acids needed to respond to starvation.

摘要

无机多聚磷酸盐（polyP）是一种由数百个磷酸（Pi）残基组成的聚合物，在大肠杆菌中会因包括氨基酸饥饿在内的应激反应而积累。在此我们表明，依赖腺苷5'-三磷酸的蛋白酶Lon与polyP形成复合物，并降解了包括S2、L9和L13在内的大部分核糖体蛋白。纯化后的S2也与polyP结合，并在有polyP存在的情况下与Lon形成复合物。因此，polyP可能会促进Lon蛋白酶对核糖体蛋白的降解，从而提供应对饥饿所需的氨基酸。