The uncharacterized transcription factor YdhM is the regulator of the nemA gene, encoding N-Ethylmaleimide reductase

被引:50
作者
Umezawa, Yoshimasa [1 ]
Shimada, Tomohiro [1 ]
Kori, Ayako [1 ]
Yamada, Kayoko [1 ]
Ishihama, Akira [1 ]
机构
[1] Hosei Univ, Dept Frontier Biosci, Tokyo 1848584, Japan
关键词
D O I
10.1128/JB.00459-08
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
N-Ethylmaleimide (NEM) has been used as a specific reagent of Cys modification in proteins and thus is toxic for cell growth. On the Escherichia coli genome, the nemA gene coding for NEM reductase is located downstream of the gene encoding an as-yet-uncharacterized transcription factor, YdhM. Disruption of the ydhM gene results in reduction of nemA expression even in the induced state, indicating that the two genes form a single operon. After in vitro genomic SELEX screening, one of the target recognition sequences for YdhM was identified within the promoter region for this ydhM-nemA operon. Both YdhM binding in vitro to the ydhM promoter region and transcription repression in vivo of the ydhM-nemA operon by YdhM were markedly reduced by the addition of NEM. Taken together, we propose that YdhM is the repressor for the nemA gene, thus hereafter designated NemR. The repressor function of NemR was inactivated by the addition of not only NEM but also other Cys modification reagents, implying that Cys modification of NemR renders it inactive. This is an addition to the mode of controlling activity of transcription factors by alkylation with chemical agents.
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页码:5890 / 5897
页数:8
相关论文
共 29 条
[1]   Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction [J].
Ackerley, DF ;
Gonzalez, CF ;
Keyhan, M ;
Blake, R ;
Matin, A .
ENVIRONMENTAL MICROBIOLOGY, 2004, 6 (08) :851-860
[2]   Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli:: Evidence for optimal activation by nickel ions [J].
Clugston, SL ;
Barnard, JFJ ;
Kinach, R ;
Miedema, D ;
Ruman, R ;
Daub, E ;
Honek, JF .
BIOCHEMISTRY, 1998, 37 (24) :8754-8763
[3]   STRUCTURE OF SHOWDOMYCIN A NOVEL CARBON-LINKED NUCLEOSIDE ANTIBIOTIC RELATED TO URIDINE [J].
DARNALL, KR ;
TOWNSEND, LB ;
ROBINS, RK .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1967, 57 (03) :548-&
[4]   INVITRO SELECTION OF RNA MOLECULES THAT BIND SPECIFIC LIGANDS [J].
ELLINGTON, AD ;
SZOSTAK, JW .
NATURE, 1990, 346 (6287) :818-822
[5]   Escherichia coli has multiple enzymes that attack TNT and release nitrogen for growth [J].
Gonzalez-Perez, M. Mar ;
van Dillewijn, Pieter ;
Wittich, Rolf-M. ;
Ramos, Juan L. .
ENVIRONMENTAL MICROBIOLOGY, 2007, 9 (06) :1535-1540
[6]  
ISHIHAMA A, 1969, J BIOL CHEM, V244, P6680
[7]   Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: Intracellular levels of four species of sigma subunit under various growth conditions [J].
Jishage, M ;
Iwata, A ;
Ueda, S ;
Ishihama, A .
JOURNAL OF BACTERIOLOGY, 1996, 178 (18) :5447-5451
[8]   The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli [J].
MacLean, MJ ;
Ness, LS ;
Ferguson, GP ;
Booth, IR .
MOLECULAR MICROBIOLOGY, 1998, 27 (03) :563-571
[9]   Fractionation of Escherichia coli cell populations at different stages during growth transition to stationary phase [J].
Makinoshima, H ;
Nishimura, A ;
Ishihama, A .
MOLECULAR MICROBIOLOGY, 2002, 43 (02) :269-279
[10]  
Miura K, 1997, BIOL PHARM BULL, V20, P110