Control of gene expression by FNR-like proteins in facultatively anaerobic bacteria

被引:6
作者
Mazoch, J [1 ]
Kucera, I [1 ]
机构
[1] Masaryk Univ, Fac Sci, Dept Biochem, Brno 61137, Czech Republic
关键词
D O I
10.1007/BF02817665
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Facultatively anaerobic bacteria are able to adapt to many different growth conditions. Their capability to change their metabolism optimally is often ensured by FNR-like proteins. The FNR protein of Escherichia colt functions as the main regulator during the aerobic-to-anaerobic switch. Low oxygen tensions activate this protein which is expressed constitutively and is inactive under aerobic conditions. The active form is dimeric and contains a [4Fe-4S](2+) cluster. The direct dissociation of the cluster to the [2Fe-2S](2+) cluster by the effect of oxygen leads to destabilization of the FNR dimer and to loss of its activity. The active FNR induces the expression of many anaerobic genes; the set comprises over 100 of controlled genes. Many other bacteria contain one or more FNR analogues. All these proteins form the FNR family of regulatory proteins. Properties of these proteins are very distinct, sometimes even among representatives of different strains of the same bacterial species. FNR-like proteins together with other regulators (e.g., two-component system ArcBA, nitrate-sensing system NarXL, etc.) control a complicated network of modulons that is characteristic for every species or even strain and enables fine tuning of gene expression.
引用
收藏
页码:95 / 103
页数:9
相关论文
共 48 条
  • [21] Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O-2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity
    Khoroshilova, N
    Popescu, C
    Munck, E
    Beinert, H
    Kiley, PJ
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (12) : 6087 - 6092
  • [22] ASSOCIATION OF A POLYNUCLEAR IRON-SULFUR CENTER WITH A MUTANT FNR PROTEIN ENHANCES DNA-BINDING
    KHOROSHILOVA, N
    BEINERT, H
    KILEY, PJ
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (07) : 2499 - 2503
  • [23] FNR MUTANTS THAT ACTIVATE GENE-EXPRESSION IN THE PRESENCE OF OXYGEN
    KILEY, PJ
    REZNIKOFF, WS
    [J]. JOURNAL OF BACTERIOLOGY, 1991, 173 (01) : 16 - 22
  • [24] KUCERA I, 1994, BIOCHEM MOL BIOL INT, V32, P245
  • [25] MUTANTS OF ESCHERICHIA-COLI-K12 UNABLE TO USE FUMARATE AS AN ANAEROBIC ELECTRON-ACCEPTOR
    LAMBDEN, PR
    GUEST, JR
    [J]. JOURNAL OF GENERAL MICROBIOLOGY, 1976, 97 (DEC): : 145 - 160
  • [26] DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    Lazazzera, BA
    Beinert, H
    Khoroshilova, N
    Kennedy, MC
    Kiley, PJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (05) : 2762 - 2768
  • [27] Bradyrhizobium japonicum FixK2, a crucial distributor in the FixLJ-dependent regulatory cascade for control of genes inducible by low oxygen levels
    Nellen-Anthamatten, D
    Rossi, P
    Preisig, O
    Kullik, I
    Babst, M
    Fischer, HM
    Hennecke, H
    [J]. JOURNAL OF BACTERIOLOGY, 1998, 180 (19) : 5251 - 5255
  • [28] Mossbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli
    Popescu, CV
    Bates, DM
    Beinert, H
    Münck, E
    Kiley, PJ
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (23) : 13431 - 13435
  • [29] Regulation of Pseudomonas aeruginosa hemF and hemN by the dual action of the redox response regulators Anr and Dnr
    Rompf, A
    Hungerer, C
    Hoffmann, T
    Lindenmeyer, M
    Römling, U
    Gross, U
    Doss, MO
    Arai, H
    Igarashi, Y
    Jahn, D
    [J]. MOLECULAR MICROBIOLOGY, 1998, 29 (04) : 985 - 997
  • [30] INVIVO AND INVITRO MUTANTS OF FNR THE ANAEROBIC TRANSCRIPTIONAL REGULATOR OF ESCHERICHIA-COLI
    SHARROCKS, AD
    GREEN, J
    GUEST, JR
    [J]. FEBS LETTERS, 1990, 270 (1-2) : 119 - 122