DNA target sequence and FNR-dependent gene expression

被引:26
作者
Scott, C [1 ]
Partridge, JD [1 ]
Stephenson, JR [1 ]
Green, J [1 ]
机构
[1] Univ Sheffield, Krebs Inst Biomol Res, Dept Mol Biol & Biotechnol, Western Bank, Sheffield S10 2TN, S Yorkshire, England
基金
英国生物技术与生命科学研究理事会;
关键词
cAMP receptor protein-FNR family; oxygen sensing; transcriptional regulation;
D O I
10.1016/S0014-5793(03)00312-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
FNR proteins are global transcription regulators that respond to fluctuations in environmental oxygen. They recognise a DNA target consisting of an inverted repeat, TTGA-TN(1)N(2)N(3)N(4)ATCAA (where N1-4 represents a non-conserved tetrad, NCT). Analysis of 68 known and predicted FNR sites from the Escherichia coli K12 genome revealed a bias toward A or T at positions N-2 and N-3 of the NCT. The effect of the NCT sequence on FNR-dependent transcription in vivo was assessed using a series of class II and class I model promoters with different NCT sequences. Changing the NCT sequence did not affect basal activity but altered anaerobic induction by as much as an order of magnitude. Thus, the NCT sequence is a fundamental component in setting the dynamic range of the FNR switch. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:97 / 101
页数:5
相关论文
共 47 条
[11]   LACK OF REDOX CONTROL OF THE ANAEROBICALLY-INDUCED NIRB+ GENE OF ESCHERICHIA-COLI K-12 [J].
GRIFFITHS, L ;
COLE, JA .
ARCHIVES OF MICROBIOLOGY, 1987, 147 (04) :364-369
[12]   FNR is a direct oxygen sensor having a biphasic response curve [J].
Jordan, PA ;
Thomson, AJ ;
Ralph, ET ;
Guest, JR ;
Green, J .
FEBS LETTERS, 1997, 416 (03) :349-352
[13]   ASSOCIATION OF A POLYNUCLEAR IRON-SULFUR CENTER WITH A MUTANT FNR PROTEIN ENHANCES DNA-BINDING [J].
KHOROSHILOVA, N ;
BEINERT, H ;
KILEY, PJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (07) :2499-2503
[14]  
Kiley PJ, 1998, FEMS MICROBIOL REV, V22, P341, DOI 10.1016/S0168-6445(98)00022-9
[15]   Recognition of DNA structure by 434 repressor [J].
Koudelka, GB .
NUCLEIC ACIDS RESEARCH, 1998, 26 (02) :669-675
[16]   DNA TWISTING AND THE EFFECTS OF NONCONTACTED BASES ON AFFINITY OF 434 OPERATOR FOR 434 REPRESSOR [J].
KOUDELKA, GB ;
CARLSON, P .
NATURE, 1992, 355 (6355) :89-91
[17]   Characterization of activating region 3 from Escherichia coli FNR [J].
Lamberg, KE ;
Luther, C ;
Weber, KD ;
Kiley, PJ .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 315 (03) :275-283
[18]   FNR-dependent activation of the class II dmsA and narG promoters of Escherichia coli requires FNR-activating regions 1 and 3 [J].
Lamberg, KE ;
Kiley, PJ .
MOLECULAR MICROBIOLOGY, 2000, 38 (04) :817-827
[19]   DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen [J].
Lazazzera, BA ;
Beinert, H ;
Khoroshilova, N ;
Kennedy, MC ;
Kiley, PJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (05) :2762-2768
[20]   THE ACTIVITY OF THE ESCHERICHIA-COLI TRANSCRIPTION FACTOR FNR IS REGULATED BY A CHANGE IN OLIGOMERIC STATE [J].
LAZAZZERA, BA ;
BATES, DM ;
KILEY, PJ .
GENES & DEVELOPMENT, 1993, 7 (10) :1993-2005