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Proteome of HU-Lacking E. coli Studied by Means of 2D Gel Electrophoresis
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...
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Published in: | Russian journal of bioorganic chemistry 2019-09, Vol.45 (5), p.366-373 |
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Main Authors: | , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 1068-1620 1608-330X |
DOI: | 10.1134/S1068162019050029 |