Proteome of HU-Lacking E. coli Studied by Means of 2D Gel Electrophoresis
- Authors: Kamashev D.E.1,2, Rakitina T.V.1,3, Matyushkina D.S.4, Evsyutina D.V.4, Vanyushkina A.A.4, Agapova Y.K.3, Anisimova V.E.2, Drobyshev A.L.2, Butenko I.O.4, Pobeguts O.V.4, Fisunov G.Y.4
-
Affiliations:
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
- Sechenov First Moscow State Medical University
- National Research Center Kurchatov Institute
- Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
- Issue: Vol 45, No 5 (2019)
- Pages: 366-373
- Section: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/229220
- DOI: https://doi.org/10.1134/S1068162019050029
- ID: 229220
Cite item
Abstract
Histone-like protein HU is a dimeric nucleoid-associated protein (NAP). HU is the most conserved NAP. It binds nonspecifically to duplex DNA with a preference for targeting nicked and bent DNA. HU limits the architecture of the bacterial nucleoid and its deletion is lethal for Bacillus subtilis and Mycoplasma genitalium which do not contain other NAPs. E. coli lacking HU is viable but has numerous growth defects. The effects of the HU protein on gene expression is known from microarray analysis and HU regulons were identified. In HU-deficient E. coli, absence of this DNA architectural protein causes a disorder in gene regulation; on the other hand, E. coli growth under standard conditions is almost unaltered in the absence of HU. To understand how the bacterium confronts the chromosomal disorder, we performed proteome analysis to compare protein abundances in cells containing the HU protein or not. Comparison of the proteomic profile of wild-type and HU-deficient E. coli shows how the altered gene expression influences the protein content. We show that proteome profile changes are very similar to the gene expression profile changes in HU-deficient E. coli. Several exceptions show that proteome studies are very important.
About the authors
D. E. Kamashev
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences; Sechenov First Moscow State Medical University
Author for correspondence.
Email: dkamashev@gmail.com
Russian Federation, Moscow, 117997; Moscow, 119146
T. V. Rakitina
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences; National Research Center Kurchatov Institute
Email: dkamashev@gmail.com
Russian Federation, Moscow, 117997; Moscow, 123098
D. S. Matyushkina
Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119435
D. V. Evsyutina
Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119435
A. A. Vanyushkina
Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119435
Yu. K. Agapova
National Research Center Kurchatov Institute
Email: dkamashev@gmail.com
Russian Federation, Moscow, 123098
V. E. Anisimova
Sechenov First Moscow State Medical University
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119146
A. L. Drobyshev
Sechenov First Moscow State Medical University
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119146
I. O. Butenko
Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119435
O. V. Pobeguts
Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119435
G. Y. Fisunov
Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency
Email: dkamashev@gmail.com
Russian Federation, Moscow, 119435
Supplementary files
