EVIDENCE FOR 5 DIVERGENT THIOREDOXIN-H SEQUENCES IN ARABIDOPSIS-THALIANA

被引:117
作者
RIVERAMADRID, R
MESTRES, D
MARINHO, P
JACQUOT, JP
DECOTTIGNIES, P
MIGINIACMASLOW, M
MEYER, Y
机构
[1] UNIV PERPIGNAN, PHYSIOL & BIOL MOLEC PLANTES LAB, CNRS, URA 565, F-66860 PERPIGNAN, FRANCE
[2] INST BIOTECHNOL PLANTES, F-91405 ORSAY, FRANCE
关键词
D O I
10.1073/pnas.92.12.5620
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Five different clones encoding thioredoxin homologues were isolated from Arabidopsis thaliana cDNA libraries. On the basis of the sequences they encode divergent proteins, but all belong to the cytoplasmic thioredoxins h previously described in higher plants, The five proteins obtained by overexpressing the coding sequences in Escherichia coli present typical thioredoxin activities (NADP(+)-malate dehydrogenase activation and reduction by Arabidopsis thioredoxin reductase) despite the presence of a variant active site, Trp-Cys-Pro-Pro-Cys, in three proteins in place of the canonical Trp-Cys-Gly-Pro-Cys sequence described for thioredoxins in prokaryotes and eukaryotes. Southern blots show that each cDNA is encoded by a single gene but suggest the presence of additional related sequences in the Arabidopsis genome. This very complex diversity of thioredoxins h is probably common to all higher plants, since the Arabidopsis sequences appear to have diverged very early, at the beginning of plant speciation. This diversity allows the transduction of a redox signal into multiple pathways.
引用
收藏
页码:5620 / 5624
页数:5
相关论文
共 42 条
  • [1] THE ARABIDOPSIS-THALIANA APURINIC ENDONUCLEASE ARP REDUCES HUMAN TRANSCRIPTION FACTORS FOS AND JUN
    BABIYCHUK, E
    KUSHNIR, S
    VANMONTAGU, M
    INZE, D
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (08) : 3299 - 3303
  • [2] BRUGIDOU C, 1993, MOL GEN GENET, V238, P25
  • [3] REGULATION OF THE FORMATION AND UTILIZATION OF PHOTOSYNTHATE IN LEAVES
    CSEKE, C
    BUCHANAN, BB
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 853 (01) : 43 - 63
  • [4] DECOTTIGNIES P, 1991, EUR J BIOCHEM, V198, P287
  • [5] DELAMOTTEGUERY F, 1991, EUR J BIOCHEM, V196, P287
  • [6] Dellaporta S.L., 1983, PLANT MOL BIOL REP, V1, P19, DOI [10.1007/BF02712670, DOI 10.1007/BF02712670]
  • [7] FERREDOXIN THIOREDOXIN REDUCTASE, AN IRON-SULFUR ENZYME LINKING LIGHT TO ENZYME REGULATION IN OXYGENIC PHOTOSYNTHESIS - PURIFICATION AND PROPERTIES OF THE ENZYME FROM C-3, C-4, AND CYANOBACTERIAL SPECIES
    DROUX, M
    JACQUOT, JP
    MIGINACMASLOW, M
    GADAL, P
    HUET, JC
    CRAWFORD, NA
    YEE, BC
    BUCHANAN, BB
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1987, 252 (02) : 426 - 439
  • [8] EKLUND H, 1984, EMBO J, V3, P1144
  • [9] FULL-LENGTH CDNA SEQUENCES FOR BOTH FERREDOXIN-THIOREDOXIN REDUCTASE SUBUNITS FROM SPINACH (SPINACIA-OLERACEA L)
    FALKENSTEIN, E
    VONSCHAEWEN, A
    SCHEIBE, R
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1994, 1185 (02): : 252 - 254
  • [10] AN NADP THIOREDOXIN SYSTEM IN LEAVES - PURIFICATION AND CHARACTERIZATION OF NADP-THIOREDOXIN REDUCTASE AND THIOREDOXIN-H FROM SPINACH
    FLORENCIO, FJ
    YEE, BC
    JOHNSON, TC
    BUCHANAN, BB
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1988, 266 (02) : 496 - 507