Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-terminal HPt domains of the sensor proteins

被引:58
作者
Perraud, AL
Kimmel, B
Weiss, V
Gross, R
机构
[1] Univ Wurzburg, Lehrstuhl Mikrobiol, Theodor Boveri Inst, Biozentrum, D-97074 Wurzburg, Germany
[2] Univ Konstanz, Fak Biol, D-78434 Constance, Germany
关键词
D O I
10.1046/j.1365-2958.1998.00716.x
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
Despite the presence of highly conserved signalling modules, significant cross-communication between different two-component systems has only rarely been observed. Domain swapping and the characterization of liberated signalling modules enabled us to characterize in vitro the protein domains that mediate specificity and are responsible for the high fidelity in the phosphorelay of the unorthodox Bvg and Evg two-component systems. Under equimolar conditions, significant in vitro phosphorylation of purified BvgA and EvgA proteins was only obtained by their histidine kinases, BvgS and EvgS respectively. One hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain (BvgS-TO-EvgS-R) was able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains (BvgS-T-EvgS-RO) was unable to phosphorylate BvgA but efficiently phosphorylated EvgA. These results demonstrate that the C-terminal HPt domains of the sensor proteins endow the unorthodox two-component systems with a high specificity for the corresponding regulator protein. In the case of the response regulators, the receiver but not the output domains contribute to the specific interaction with the histidine kinases, because a hybrid protein consisting of the EvgA receiver and the BvgA output domain could only be phosphorylated by the EvgS protein.
引用
收藏
页码:875 / 887
页数:13
相关论文
共 37 条
  • [1] ECTOPIC EXPRESSION OF THE FLAGELLAR REGULON ALTERS DEVELOPMENT OF THE BORDETELLA HOST INTERACTION
    AKERLEY, BJ
    COTTER, PA
    MILLER, JF
    [J]. CELL, 1995, 80 (04) : 611 - 620
  • [2] ALEX AL, 1996, P NATL ACAD SCI USA, V98, P3416
  • [3] Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    Appleby, JL
    Parkinson, JS
    Bourret, RB
    [J]. CELL, 1996, 86 (06) : 845 - 848
  • [4] SEQUENCES REQUIRED FOR EXPRESSION OF BORDETELLA-PERTUSSIS VIRULENCE FACTORS SHARE HOMOLOGY WITH PROKARYOTIC SIGNAL TRANSDUCTION PROTEINS
    ARICO, B
    MILLER, JF
    ROY, C
    STIBITZ, S
    MONACK, D
    FALKOW, S
    GROSS, R
    RAPPUOLI, R
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1989, 86 (17) : 6671 - 6675
  • [5] IN-VIVO CHARACTERIZATION OF THE UNORTHODOX BVGS 2-COMPONENT SENSOR PROTEIN OF BORDETELLA-PERTUSSIS
    BEIER, D
    SCHWARZ, B
    FUCHS, TM
    GROSS, R
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1995, 248 (03) : 596 - 610
  • [6] Conserved sequence motifs in the unorthodox BvgS two component sensor protein of Bordetella pertussis
    Beier, D
    Deppisch, H
    Gross, R
    [J]. MOLECULAR & GENERAL GENETICS, 1996, 252 (1-2): : 169 - 176
  • [7] A FULLY MODULAR VECTOR SYSTEM FOR THE OPTIMIZATION OF GENE-EXPRESSION IN ESCHERICHIA-COLI
    BELEV, TN
    SINGH, M
    MCCARTHY, JEG
    [J]. PLASMID, 1991, 26 (02) : 147 - 150
  • [8] Bordet J., 1909, ANN I PASTEUR PARIS, V23, P415
  • [9] THE MODULAR ARCHITECTURE OF BACTERIAL RESPONSE REGULATORS - INSIGHTS INTO THE ACTIVATION MECHANISM OF THE BVGA TRANSACTIVATOR OF BORDETELLA-PERTUSSIS
    BOUCHER, PE
    MENOZZI, FD
    LOCHT, C
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1994, 241 (03) : 363 - 377
  • [10] A PHASE VARIANT OF BORDETELLA-PERTUSSIS WITH A MUTATION IN A NEW LOCUS INVOLVED IN THE REGULATION OF PERTUSSIS TOXIN AND ADENYLATE-CYCLASE TOXIN EXPRESSION
    CARBONETTI, NH
    KHELEF, N
    GUISO, N
    GROSS, R
    [J]. JOURNAL OF BACTERIOLOGY, 1993, 175 (20) : 6679 - 6688